WO2012121612A1 - Procédé de fabrication d'une composition comestible - Google Patents

Procédé de fabrication d'une composition comestible Download PDF

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Publication number
WO2012121612A1
WO2012121612A1 PCT/NZ2012/000027 NZ2012000027W WO2012121612A1 WO 2012121612 A1 WO2012121612 A1 WO 2012121612A1 NZ 2012000027 W NZ2012000027 W NZ 2012000027W WO 2012121612 A1 WO2012121612 A1 WO 2012121612A1
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Prior art keywords
hydrolysate
meat
protein
hydrolysis
temperature
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PCT/NZ2012/000027
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English (en)
Inventor
Shantanu Das
Harjinder Singh
Paul James Moughan
Sharon James HENARE
Jian Cui
Brian Herbert Patrick Wilkinson
Robert Chong
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Meat Biologics Research Limited
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Publication of WO2012121612A1 publication Critical patent/WO2012121612A1/fr

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    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J3/00—Working-up of proteins for foodstuffs
    • A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
    • A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
    • A23J3/34—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes
    • A23J3/341—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of animal proteins
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
    • A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
    • A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
    • A23L33/17—Amino acids, peptides or proteins
    • A23L33/18—Peptides; Protein hydrolysates

Definitions

  • This invention relates to the manufacture of an edible composition.
  • the present invention relates particularly to edible compositions in the form of hydrolysates which are hydrolyzed bio-matter typically prepared into compositions for human consumption.
  • Hydrolysates can be used for nutrient supplements for bodybuilders and endurance athletes, nutritional support of the malnourished including ⁇ cancer patients, elderly and post-operative patients, pregnancy nutritional support, weight control or treating malnutrition in AIDS patients, and so forth.
  • the usefulness of hydrolysates stems from the compositions containing nutrients that can aid the recovery, maintenance and improvement of human health.
  • hydrolysates have been prepared from whey, milk or soy; partially due to their characteristic cost-effectiveness and availability.
  • increasing demands in these industries have resulted in an increased price of these commodities. This can lead to an increased cost of the product for the end- consumer.
  • the nutrients available from these sources often do not effectively match the nutrient requirements of the human body. This is particularly so in case of elderly people who have high requirements for amino acids.
  • a large volume of hydrolysate must be consumed. This is often undesirable, as many elderly people (for example) may not be able to consume large amounts of the composition due to reduced diet intake.
  • other undesirable food components e.g. fat, salt, sugars, flavourings or preservatives
  • Some nutrients e.g. essential amino acids
  • hydrolysates e.g. those from vegetable sources.
  • Amino acids play an important role in human body by acting as building blocks for tissues.
  • the techniques used to prepare the hydrolysate can be detrimental to the resulting nutrient levels in the composition, where the nutrients can be lost during the processing steps, leading to loss of nutritional value of the final product.
  • many hydrolysates can have a short shelf life, and many of the nutrients can be lost during storage. This can lead to a reduction in their effectiveness upon consumption by the user.
  • hydrolysates can have undesirable flavour profiles. Often the flavour level can be overbearingly salty or bitter. In order to overcome unpalatable flavours of the hydrolysates, synthetic flavouring is often added. This can be a further disadvantage as people prefer natural products lacking synthetic additives.
  • Some materials sourced for preparing hydrolysates can also represent a hazard for disease transmission.
  • the regulations can be ineffective to prevent disease transmission through human consumption of animal products.
  • Diseases that are transmitted through an animal population e.g. Bovine Spongiform Encephalopathy, or "Mad Cow Disease” in cattle
  • Radical treatment means can often be required to ensure the disease is not transmitted to humans.
  • the consumer's trust in the meat quality can make commercialization non-viable. Therefore, it is critical to identify a source, that not only has stringent regulatory approval, but also has consumer confidence.
  • nutrients within the hydrolysates can be poorly absorbed by the body, or are absorbed at the inappropriate position within the digestive tract. This is often a result of poor pharmacokinetic properties of the composition (e.g solubility levels, pH suitability, and absorption across the intestinal tract). Absorbtion is also highly dependent on the source and method of preparation. This is a major concern as the consumer may falsely believe they are receiving adequate levels of the nutrient (as labeled on the product) when in fact they are not.
  • the timeframe of the hydrolysis must be closely monitored. Alterations in the source and type of meat source can dramatically affect the timeframe required for adequate hydrolysis. Furthermore, the purpose of the product must be considered when assessing the timeframe of the hydrolysis. The level of hydrolysis can also affect flavour e.g. hydrolysis can lead to generation of bitter peptides. As such many variables must be considered when determining the appropriate length of hydrolysis. Also an additional hydrolysis step may be required to remove unwanted components. This can take up valuable time, equipment and/or can lead to a reduction of nutrients lost during the additional hydrolysis step
  • hydrolysates are not well adapted for numerous purposes. Often, the hydrolysates can be well suited to one given purpose (due to high levels of a particular nutrient), but can be rather ineffective for other purposes. It has been a goal to develop a well-rounded hydrolysate that may be used effectively either as a supplement or to treat multiple ailments.
  • a method of preparing a hydrolysate composition from a meat source including the steps of: a) hydrolysing at least one type of protein in the meat source, b) restricting the hydrolysis process to form a hydrolysate mixture, characterised by the further step of c) sourcing the protein from mechanically separated meat.
  • dietary protein quality are of fundamental importance in nutrition.
  • the nutritional value of dietary proteins depends on the composition of amino acids and their bioavailability for metabolic utilization. The latter is determined by digestion and absorption processes in the gastrointestinal tract. As we age, the ability to eat and digest proteins is reduced in some people. This is due to many reasons including changes in taste and smell, poor oral health resulting in difficulties with chewing and/or swallowing, decreased appetite and reduced food intake. This reduced food intake is an important issue because it may lead to protein-energy malnutrition is correlated with a higher rate of mortality and morbidity. Protein-energy malnutrition accentuates the physiological loss of skeletal muscle mass that occurs with advancing age, known as sarcopenia, resulting in a higher requirement for superior quality dietary protein.
  • Essential amino acids are the amino acids which must be obtained from the diet. If an individual's diet is deficient in one or more of these amino acids, the usefulness of other amino acids is affected even if they are present in otherwise sufficient quantities.
  • targeted amino acid supplementation may indeed be beneficial in cases involving accelerated protein catabolism (e.g. advanced sarcopenia, cachexia and trauma) for the majority of older adults, a current method of increasing skeletal muscle protein anabolism is to include a serving of protein of high biological value during each meal (Paddon-Jones et a/. 2008).
  • the current invention provides an efficient and practical means to provide high biological value protein in a hydrolysate for humans or other animals either who are deprived of some or all amino acids, or require supplements for growth and development.
  • This hydrolysate is prepared from mechanically separated (MS) meat, a starting material that otherwise is typically discarded. Furthermore, the hydrolysate in the current invention is preferably prepared in a format that is easy to consume and is pleasant to eat.
  • hydrolysate may have low levels of undesirable components such as fats whilst still maintaining high protein levels and an optimal amino acid profile.
  • hydrolysate should be taken to mean any biological material that has been hydrolysed, digested, cleaved or metabolised either enzymatically or non-enzymatically, into smaller components than normally present in the un-modified biological material.
  • a meat source will include proteins, otherwise known as polypeptides.
  • a polypeptide is a chain of amino acids linked by peptide bonds. When a polypeptide is hydrolysed (i.e. cleaved), it may be cleaved into shorter polypeptide chains with varying number of amino acids or single amino acids depending on the extent of hydrolysis.
  • composition should be taken to mean any mixture intended for human consumption or application in order to provide a beneficial effect.
  • meal source should be taken as meaning any biological resource sourced from an animal.
  • protease should be taken as meaning any protein with enzymatic activity, wherein the enzymatic activity relates to the cleavage of molecular bonds between two adjacent amino acids in a polypeptide chain.
  • MS meat should be taken as meaning any meat source that requires a tool to isolate it from the meat source itself.
  • the "mechanically separated (MS) meat” utilises lower grade meat not normally used for human consumption, due to unwanted characteristics (for example, small sizes of the meat, poor appearance, flavour or texture profiles).
  • MS meat As a starting material for the hydrolysate, there are a number of considerable advantages in using MS meat as a starting material for the hydrolysate, including: a) Easy to source (this is material that would typically be discarded and not used for normal consumption by humans. Also being a by-product its cost is very low leading to lower cost of the end product for consumers. b) provides added value to the MS meat (e.g.
  • MS meat may effectively treat a number of conditions and diseases as well as acting as an effective nutritional supplement for health maintenance, development or disease prevention.
  • MS meat is generally not used for consumption by humans because of its poor flavour and texture characteristics but can be utilized to produce a protein hydrolysate which has superior flavour profile and is rich in amino acids.
  • the meat source is lamb.
  • other sources of protein including but not limited to, meat sources like cow, goat, deer, rabbit etc. may be suitable.
  • the inventors have found that lamb meat may provide particularly advantageous levels of nutrients (e.g. amino acid profile) which closely match what may be required by the human body during growth and development, recovery and/or treatment. There is convincing support that amino acids play an important role in enhancing human muscle repair and growth
  • the meat source is from New Zealand.
  • New Zealand has a strong regulatory system and is relatively disease free, there is less likelihood of the meat source harbouring disease.
  • the inventors have found that typically 250 kg of MS meat may be required to generate 15 kg hydrolysate. The inventors acknowledge that if more or less hydrolysate is required, the amount of starting material may be adjusted accordingly. Processing large amounts of meat in batch production adds an element of complexity to the present invention. Even minor variations in the conditions may have a dramatic effect on the results.
  • hydrolysis conditions have been standardized after a series of experiments. However, a skilled person would appreciate that depending on the starting material and the results desired, the conditions chosen may be altered substantially.
  • hydrolysis of meat is achieved partly due to the use of proteases.
  • MS meat is minced prior to the addition of protease(s).
  • This step provides a greater surface area/volume ratio on the MS meat such that the protease(s) have better access to the meat. This helps improve the efficiency of the hydrolysis step.
  • the MS meat is suspended in water and maintained at a temperature of approximately 45°C prior to the addition of protease(s). This may help to soften the meat prior to hydrolysis beginning, and thereby improving efficiency of the process.
  • a combination of proteases are added to the MS meat. The inventors have found that the combination of Protamex ® and Flavourzyme ® is particularly effective in hydrolysing the meat source.
  • the combination of proteases are added simultaneously to the MS meat suspension.
  • the inventors have found that adding the proteases simultaneously improves the manufacturing efficiency of hydrolysate.
  • the enzymes are typically added to the starting material in a step-by- step fashion.
  • a step by step hydrolysis requires longer time as separate incubation times would be required and hence the efficiency of manufacturing would be greatly reduced.
  • the hydrolysis step is performed at a temperature between 40 - 50°C. Most preferably the temperature is 45°C. This temperature was found to be particularly effective for optimal enzymatic activity. This may help to improve the efficiency of hydrolysis.
  • the hydrolysis step is performed at a pH of approximately 5.0 - 8.0. Most preferably, the pH is at 6.5.
  • the hydrolysis step may continue for substantially any length of time. However the inventors have found that a time period of between 2 - 5 hours may be appropriate to provide a desired level of protein hydrolysis. Preferably, the hydrolysis step continues for 3.5 hours.
  • the inventors consider it preferable to have a high degree of hydrolysis. This may be largely dependent on the length of time the proteases are allowed to digest the protein before the proteases are inactivated. However many variables need to be standardized for getting optimum degree of hydrolysis such as pH and hydrolysis temperature. A high degree of hydrolysis is likely to play an important part in achieving the excellent absorption characteristics of the hydrolysate (described in detail in the Best Modes section).
  • the inventors aim to have approximately 70- 90% of the resulting peptides below a size of 1000 Daltons. Similarly, this equates to having a large proportion of di- and tri- peptides in the hydrolysate.
  • amino acid profile of the hydrolysate may be altered in numerous ways.
  • different meat sources may be used, such as cattle, sheep, or poultry and pigs
  • different parts of an animal may be used.
  • Each component may have variations in the amino acid profile, which may be tailored to a given condition or animal to be treated. crucial to appreciate that in preferred embodiments the hydrolysate will have a high protein level (60-90%), however the subtle differences in amino acid balance may be altered to suit different needs.
  • An alternative method to tailor the amino acid profile may be to vary the hydrolysis conditions. For example, one may alter the timeframe of the hydrolysis reaction, amount or types of protease(s), or temperature of the reaction to change the degree of hydrolysis of the meat source.
  • the inventors also envision that it may be viable to add exogenous amino acid(s) to the hydrolysate for a particular formulation. For instance, a given meat source may be deficient in one or more amino acids even though it represents a good source of protein and has other beneficial characteristics for the hydrolysate.
  • the inventors have found that the timeframe of the hydrolysis reaction is important. A reaction that persists for too long (e.g. beyond five hours), the resulting hydrolysate may have an unpalatable taste due to the release of different peptides and amino acids.
  • the time for hydrolysis is standardized based on series of experiments with different enzymes, singly or in combination and resulting flavour and nutritional profiles in the hydrolysate.
  • a precipitate may form in the reaction mixture. Precipitate is the insoluble part of the material, which may cause problems during final product manufacture (e.g. RTD soup formulated with lamb protein hydrolysate).
  • One possible reason for formation of precipitate is denaturation of protein if processed for too long.
  • a further outcome of continuing the hydrolysis step for too long may be that the amino acid profile changes as a result of the connective tissue starting to get hydrolysed. This may change the amino acid profile such that it may not be well matched for a particular use.
  • the hydrolysis step is ended too soon (e.g. less than 2 hours) the degree of hydrolysis would not be adequate resulting in larger polypeptides (e.g. over 1000 Da) This may reduce the absorption of some or all types of amino acids within the hydrolysate, especially if the consumer is unable to effectively digest the polypeptides. Poor absorption characteristics may lead to less nutritional benefit of the hydrolysate. It is envisaged that the length of the hydrolysis step will most likely be controlled by deactivating the proteases.
  • lumps of unwanted material such as fat and connective tissue are manually removed from the mixture. This step may help to remove excess amounts of undesirable components.
  • the digested (or partially digested) protein is centrifuged. This may be useful to further remove unwanted fats and / or other solids (e.g. connective tissue).
  • the present method may allow a by-product previously seen as waste be converted into a hydrolysate with high levels of protein and an excellent amino acid profile with low levels of fats (e.g. 0.4 % w/w).
  • hydrolysates currently available have a relatively high level of fat. This can often be due to difficulty in removing the fats from the other components. Furthermore, the fats may be retained or added to the hydrolysate to improve flavour etc.
  • the present invention is particularly advantageous as the fats may be effectively removed without losing the good palatability characteristics of the hydrolysate sourced from meat.
  • fats may be selectively removed while also maintaining a high protein level and an excellent amino acid profile.
  • Hydrolysates sourced from - other sources like vegetable sources for example are claimed to be high in protein content, low in fat content- similar to the features in the present invention.
  • these hydrolysates may not have all the amino acids for human requirements and may have an unpleasant flavour.
  • a supernatant resulting from the centrifugation step is collected and used for further processing of the hydrolysate.
  • the step of deactivating the protease(s) includes heating the mixture to a temperature and time sufficient to denature the protease(s).
  • the inventors have found that heating the hydrolysis mixture (containing the proteases) for approximately 10 minutes at a temperature of at least 75°C. Heating the hydrolysate mixture may also be advantageous as it may simultaneously act as a means to pasteurise the hydrolysate.
  • deactivation step is not restricted to heat treatment and other methods of enzyme deactivation known in the art are also considered acceptable.
  • the deactivation step may take place in a water jacketed vessel to maintain a high temperature.
  • the deactivated hydrolysate mixture is concentrated to a solid content of approximately 30 - 40%.
  • Numerous methods may be used to concentrate the hydrolysis suspension. The inventors have found that a particularly preferred method uses a rising film evaporator at a temperature of approximately 50°C - 70°C.
  • the concentrate is spray dried into a powder.
  • the concentrate can be dried using any drying technologies like vacuum drying and freeze drying. Drying the concentrate by spray drying is most cost effective delivering high quality and a high throughput than other methods.
  • the hydrolysate powder may then be packaged for storage.
  • hydrolysis conditions described above have been shown to provide very advantageous amino acid and molecular weight profiles as outlined in the best modes section, and may be particularly useful for a range of supplementary and therapeutic applications.
  • meat is disease-free Method may be used for batch production
  • FIG. 1 Overview of hydrolysate method of preparation
  • Figure 9 Plasma glucose concentrations after the ingestion of a mixed meal containing 5 N-labelled lamb hydrolysate or casein in older adult humans;
  • FIG. 10 Serum insulin concentrations after the ingestion of a mixed meal containing 15 N-labelled lamb hydrolysate or casein in older adult humans;
  • Figure 11 Incorporation of dietary nitrogen into serum proteins after ingestion of a mixed meal containing hydrolysed lamb meat or casein in older adult humans;
  • Figure 12 Incorporation of dietary nitrogen into body urea (A), cumulative excretion of urinary urea (B) and cumulative excretion of urinary ammonia (C) after ingestion of a mixed meal containing hydrolysed lamb meat or casein in older adult humans;
  • EXAMPLE 1 A description of the preferred hydrolysate of the present invention.
  • the hydrolysate composition is isolated from mechanically separated (MS) off-cuts of lamb meat sourced in New Zealand.
  • the hydrolysate has a protein level of 83.4% (w/w), fat level of 0.4%, moisture level of 5.0% and ash level (which is an indicator of mineral content) of 7.3%
  • the pH of the hydrolysate is 6.3 (at 10% in water at 23°C).
  • the solubility of the hydrolysate is 87% (at 1 % w/v in water).
  • the hydrolysate includes a well balanced amino acid profile (discussed further in the Examples below).
  • the hydrolysate is highly absorbable, where the mean true digestibility for all amino acids is 98%.
  • the hydrolysate has a level of hydrolysis of 40%. 90% of the protein in the hydrolysate has a molecular weight of less than 1000 Daltons. Furthermore, 78% of the peptides in the hydrolysate are less than 10 amino acids in length, and the average size of the peptides is two amino acids.
  • the hydrolysate is provided in a dry soup mix or powder.
  • other means of providing the hydrolysate may include a slurry, tablet, injecteable liquid or drink, bolus, etc or any other form of food or nutraceutical.
  • FIG. 1 shows an overview of a hydrolysate method of preparation. A more detailed method is discussed below.
  • Minced MS lamb meat was suspended in deionised water and heated to 45°C.
  • Protamex and Flavourzyme were simultaneously added to the suspension to allow the hydrolysis at 45°C under stirring for 3.5 hour.
  • the digested meat slurry was centrifuged to remove fat and un-hydrolysed solids (e.g. connective tissue).
  • the hydrolysate liquor was concentrated using a climbing film evaporator and spray dried into a light brown fine powder.
  • Table 1 List of raw materials used in manufacture of hydrolysate powder from MS
  • Table 2 List of equipment used in manufacture of hydrolysate powder from MS lamb meat
  • the hydrolysate was separated using an ultracentrifuge above 12000 *g for 5 minutes. In an industrial setting the material may need to be centrifuged in a decanter type centrifuge. ⁇ The hydrolysed meat slurry was heated to 75°C (minimum) for 10 minutes to deactivate the enzymes and to pasteurize the product. This was achieved in the water jacketed vessel. The 3.5 hour time limit for the hydrolysis is critical - as even a delay of fifteen minutes can lead to detectable bitter notes as a consequence of excessive hydrolysis. Moreover, the amino acid balance changes reasonably fast with the hydrolysis of the connective tissue. • A rising film evaporator was used to concentrate the hydrolysate liquor to a solids content of 30-40%. The exit temperature was controlled under 60°C.
  • a spray drier was applied to dry the concentrate into the powder.
  • the exit temperature was controlled at 80°C while the outlet air temperature was at 180°C.
  • CFU Colony Forming Unit
  • Water solubility measurement The measurement is based on a modified AOAC (950.81 ) method. Approximately 1 g (Ws) of MS lamb hydrolysate powder was added to 100 mL (V s ) of water in a 250 mL conical flask and shaken on a 150 rpm rotation shaker for 2 hours. About 30 mL (V c ) of the solution was centrifuged at 15000 rpm for 20 minutes. The supernatant was then dried (W d ) in a 105°C oven overnight. All the data were measured in duplicate. WS was calculated based on the following equation.
  • W d refers to the dried weight (g) of the supernatant in V c
  • W s refers to the weight (g) of the powder sample
  • V s refers to total volume (mL) of the solution
  • V c refers to the supernatant volume (mL) from centrifuge Microbiological test
  • Meat hydrolysate is highly hydrolysed with a degree of hydrolysis of around 40%. This means that more than 40% of the peptide links are severed by the hydrolysis and results in a mixture of small peptides or individual amino acids. This aids absorption of the protein and also contributes to the pleasant beefy flavour of Meat hydrolysate.
  • the aim of the trial was to assess the impact of storage conditions on the storage life and quality of Meat hydrolysate when packaged under vacuum in aluminium-foil laminated pouches. The results are presented in this report.
  • Meat hydrolysate contains a high level of protein (83.4%) and low levels of fat (0.4%) and collagen (1.5%). Colour (L. a* and b*) of Meat hydrolysate showed small changes with temperature and time.
  • the water solubility (WS) of Meat hydrolysate (87.3 ⁇ 0.7 %) showed no change with either storage time or storage temperature.
  • GC Headspace analysis released a series of characteristic peaks in the initial stage, week 12 and week 24
  • Lysine availability tended to decrease with increasing storage temperature and storage time, with storage time having a greater impact on lysine loss than storage temperature. The lysine availability was 88% at time 0, but reduced to the range from 59 % to 67% at week 24. More in vitro available lysine was lost at 37°C than at lower temperatures.
  • Microbial counts (200-400 CFU/gm) showed little change with temperature and time.
  • An informal sensory test showed that the sensory quality of samples stored at temperatures ⁇ 20°C showed little deterioration with either storage time or temperature.
  • the powder stored at -20°C had a meatier and oilier odour than the samples stored at 4°C and 20°C for all assessments.
  • Samples stored at 37°C deteriorated slightly in terms of the taste of its 2.1% aqueous broth at the end of the trial, but the deterioration was not significant.
  • MS lamb meat was purchased from a New Zealand supplier. Packaging for storage and sampling
  • Meat hydrolysate was conditioned for 24 hours prior to packaging to allow the moisture in the spray dried powder to equilibrate. Fifteen grams of the powder were weighed into aluminium foil laminated pouches and sealed under vacuum.
  • the fifteen gram pouches were randomly selected and then allocated to a specific storage temperature.
  • the pouches were stored at the following four temperatures:
  • Proximate analysis of the product was conducted according to the following methods: total combustion method for protein content (AOAC 968.06), Soxhlet extraction for fat content (AOAC 991.36), conventional oven drying at 105°C for moisture content (AOAC 930.15, 925.10), furnace combustion at 550 °C for ash content (AOAC 942.05), Plasma Emission Spectrometry for minerals analysis, hydrochloric acid hydrolysis followed by HPLC separation for amino acids (AOAC 994.12) and alkaline hydrolysis followed by HPLC separation for tryptophan analysis.
  • WS Water solubility measurement
  • Meat hydrolysate was added to 100 mL of water in a 250 mL conical flask and shaken on a 150 rpm rotation shaker for 2 hours. About 30 mL of the solution was centrifuged at 15000 rpm for 20 minutes. The supernatant was then dried in a 105°C oven overnight. All the data were measured in duplicate.
  • WS was calculated based on the following equation.
  • W d refers to the weight (g) of dried solubles in V c W s refers to the weight (g) of the powder sample V s refers to total volume (mL) of the solution
  • V c refers to the supernatant volume (mL) from centrifuge Headspace analysis
  • a gas chromatograph was used for headspace analysis.
  • the SHIMADZU GC-2010 gas chromatograph and a SupelcowaxTM 10 fused silica capillary column (30 m x 0.32 mm ⁇ 0.50 ⁇ ) were used in the present study.
  • the CAR/PDMS fibre (75 ⁇ ) was conditioned before use and transferred into the injector port of the GC by a SHIMADZU AOA-5000 auto sampler.
  • the injector port temperature was set at 250°C, the detector at 250°C and the oven 100°C.
  • the splitless mode was used.
  • the carrier gas used was Helium supplied by BOC Gases (Palmerston North) Ltd.
  • the flow rate of the carrier and fuel gas were controlled at 2.4 mL/min.
  • Each 20 mL glass vial for holding the sample contained 2 g of the spray-dried powder and was sealed with a rubber/aluminium cap. Duplicate injections were required for the GC headspace analysis.
  • O-methylisourea (OMIU)-reactive lysine was determined using a procedure described by Moughan and Rutherfurd (1996) followed by HPLC separation. All analyses were conducted in duplicate. The samples were analyzed for total lysine and 'reactive lysine' or available lysine.
  • a conventional aerobic plate count method (Vanderzant and Splittstoesser, 1992) was applied to assess the effect of storage time and temperature on microbial quality of the stored hydrolysate powders. Samples were analysed for microbial counts in duplicates to assess microbial numbers for the four temperature treated samples at each testing time. Approximately 0.5g of the powder was taken from each pack and dissolved and then the following dilutions were performed at 1 : 50, 1 : 500 and 1 : 5000. The plate count agar used was supplied by Merck Co. of USA.
  • Meat hydrolysate contained less fat (0.4%) and more protein (83.4%) than the MS lamb meat (21.5% fat and 19.4% protein with connective tissue included).
  • Table 9 Chemical Com osition /100 of Meat h drol sate:
  • Meat hydrolysate contained 1.5% collagen, eight times lower than that in raw MS lamb meat (11.7%) About 87% of the collagen-associated connective tissue was removed through the process. Due to the fact that there was such a low level of fat in Meat hydrolysate (0.4%), TBA tests or peroxide analysis were not considered.
  • the full mineral analysis results show that the total minerals made up 6.6% of the powder, and contained high levels of chloride, potassium, sodium, sulphur, phosphorus, calcium and magnesium, low levels of iron, zinc and manganese, and trace amounts of other minerals.
  • the maximum sodium chloride level was about 2.6 g/100g of Meat hydrolysate assuming all the chloride (1.6g/100g) was bound to sodium.
  • the table below shows the amino acid contents of Meat hydrolysate and two lamb meats. There were no obvious differences between the samples. The threonine, serine, alanine, tyrosine and arginine levels were approximately 10% lower in Meat hydrolysate than in the lamb leg muscle.
  • the methionine was 35% lower in Meat hydrolysate and the valine and histidine contents, on the other hand, were 10% higher in Meat hydrolysate than the lamb leg muscle.
  • the threonine, proline, glycine and methionine levels were about 10% lower in Meat hydrolysate than in raw meat.
  • the glutamic acid, valine and lysine levels in Meat hydrolysate were about 10% greater than in the raw MS lamb meat.
  • the hydroxyproline content in Meat hydrolysate was 7.4 times lower than that in MS lamb meat and 1.8 times lower than that in lamb lean leg muscle. This implies that Meat hydrolysate has a low collagen level.
  • the L * values changed within a relatively smaller range compared to those of the samples stored at 20°C and 37°C.
  • the L* values of all the samples were at their maximum values at week 24.
  • the a* values of all the samples increased with time until week 20, with the 37°C sample having higher a * values.
  • the a * values then deceased to their minimum at the end of 24 weeks except for the sample stored at 20°C which remained unchanged after week 20.
  • the b * values of all the samples changed in a similar pattern to a * values.
  • the 37°C sample had a higher b * value than the other samples till the end.
  • the higher temperatures e.g. 37°C
  • the higher temperatures generally caused larger variations in the colour spaces over the storage period than the in the samples stored at the lower temperatures. Effect of storage on water solubility of the product
  • Water solubility (WS) of Meat hydrolysate in the test was defined as the maximum amount of the hydrolysate that could be dissolved in water at room temperature (20-24°C) and atmospheric pressure.
  • the results shown in Figure 3 indicate that the WS of the samples increased over the first 8 weeks of storage with the 20°C stored sample showing the greatest change from 86.5% to 88.0%. The solubility of all samples then remained constant until week 12 and then declined.
  • the WS of the sample stored at 37°C dropped from 88% to 86.6% by week 16. It appeared that the samples stored at 37°C had a lower WS than other samples, but this difference was only slight and had no effect on sample quality.
  • the WS at pH 2.0, 4.0, 6.3 (natural pH), 9.0 and 11.0 were also determined to observe the effects of aqueous solution pH on the WS of Meat hydrolysate stored at 20°C over a period of 6 months.
  • the results are shown in Figure 4, indicating that the WS of the samples under different pH values changed over a wider range from 82.0% to 89.8% than those solutions made from the unadjusted samples (pH 6.3). All the samples exhibited minimum WS (82.0 %) at pH 4 and were highly soluble at pH11 with the maximum WS at 89.8%.
  • Storage time had effects on the WS under different pH values, but with no regular trend except for the pH 2 samples which increased in solubility with time. Effects of the storage on volatile components of the product
  • the sample presented a series of specific peaks at 2.9, 4.9, and 8.2 minutes which were absent in the profile of air used as control.
  • the highest peak of the sample appeared at the retention time of 15.7 min with an arbitrary unit of 87,000, twice as high as obtained from the air blank (38,000 au). This component made up 34.6% and 12.1% of the total volatile components of these two samples respectively.
  • the air blank sample generated a peak of 190,000 au, making up 61.4% of its total components. No peak appeared at the corresponding time for Meat hydrolysate.
  • the major peak (809,000 au) appeared at an elution time of 5.9 min for the sample stored at -20°C, making up 52.9% of its total components. It gave a characteristic feature to the sample's chromatogram.
  • the peak height increased with storage temperatures from 116,000 au to 177,000 au. No higher peak than these appeared within the elution timeframe, except for the -20°C sample at 5.9 min.
  • the volatile components at 1.8 min could be closely associated with the flavour characters of the samples stored for a period of 12 weeks. This peak contributed 7.6%, 29%, 49% and 57% of their respective total components to the samples stored at -20°C, 4°C, 20°C and 37°C.
  • the content of available lysine is a very powerful determinant of the protein quality of a food product.
  • the free amino group of lysine in protein foods can react, for example, to form Maillard complexes with sugars that may thereby reduce the availability of lysine (Miller and Gerrard, 2005).
  • the effects of storing the hydrolysate powder at temperatures of -20°C, 4°C, 20°C and 37°C for a period of 24 weeks on lysine availability were examined.
  • results were expressed as an estimated CFU counts per gram as shown in Table 13.
  • the sample stored at 37°C showed a decreased CFU number whilst the samples stored at -20°C, 4°C and 20°C showed no change in the CFU numbers with time.
  • the plate count result indicates that the samples met "the microbiological reference criteria for food" in New Zealand (Ministry of Health of New Zealand, 1995). Clearly, microbial quality was not an issue for this product.
  • Table 13 Plate counts of Meat hydrolysate stored at four temperatures for a periods of 12, 24 weeks:
  • Meat hydrolysate contained 0.4% fat and 83.4% crude protein (includes 1.5% collagen), 7.3 % ash and 5.1 % water.
  • the sodium chloride level (assuming all the chloride was bound to sodium) was estimated to be 2.6 g/100g of the hydrolysate powder, which explains why the powder was deemed to be 'salty'.
  • Amino acid composition of Meat hydrolysate was slightly different from those for the lamb leg muscle and MS lamb meat. However, the
  • hydroxyproline content of Meat hydrolysate was 1.8 times lower than that in lamb leg muscle and 7.4 times lower than that in MS lamb meat.
  • the WS of Meat hydrolysate showed little change with either storage time or storage temperature, and was within a narrow range of 86.5% to 88.0%. pH manipulation of the samples had a much greater impact on WS than temperature with the WS ranging from 82% to 90%. All the samples exhibited a minimum WS at pH 4 and were highly soluble at pH11.
  • Total lysine was neither affected by storage time nor temperature. However, available lysine decreased with both storage time and storage temperature with storage time having the greater impact. The available lysine content decreased from about 88% at time 0 to between 58.6% - 66.8 depending on storage temperature. The higher the temperature the greater was the loss of available lysine.
  • Calculations performed using this information determined the utilization of the hydrolysate and were compared with information obtained from volunteers who received a meal containing a marked reference protein prepared from milk.
  • the objective of this study was to determine the postprandial (after meal) nitrogen utilization of a meat hydrolysate in older adults by measuring dietary nitrogen intake and absorption.
  • the study employed a state-of-the-art isotope tracer methodology.
  • the study population comprised 26 older (60 - 81 years of age), community- dwelling adults. Volunteers with a history of diabetes mellitus, bleeding disorders, cancer (any form), any gastrointestinal, hepatic or hormonal disorders or disturbances were excluded as were smokers and people who drank more than 2 units of alcohol per day. Volunteers who used medication known to influence digestion were excluded and any use of multivitamin supplements on a regular basis was stopped one week before the trial. Other exclusion criteria were vegetarians/vegans, allergies to dairy products and significant weight change during the past six months. Before study entry the volunteers provided urine and fasting blood samples that were screened for hematologic, liver and kidney function and for electrolytes. Volunteers with blood values outside the recorded reference ranges for the laboratory were excluded. Food intake was recorded for one week and protein intake calculated to ensure that protein intake was within normal guidelines for general health for an older New Zealand adult (> 51 years, NHMRC 2005). People who consumed more than the recommended daily protein intake were excluded.
  • Anthropometric measurements were taken during an initial screening visit. Height was measured by using a stadiometer to the nearest 1 cm and body mass was measured by using the BOD POD calibrated electronic weighing scale to the nearest 0.01 kg. Body composition was determined using air-displacement plethysmography (BOD POD Composition System, Life Measurement, Inc).
  • the meals were designed to be balanced providing one third of the daily recommended dietary energy intake (approximately 700 kilocalories) for an older New Zealand adult (> 51 years, NHMRC 2005).
  • the meals were formulated to provide 30 g of protein, uniformly and intrinsically labelled with 15 N.
  • the source of protein was either lamb protein hydrolysate or casein.
  • the carbohydrate and fat sources (maltodextrin and canola oil respectively) were identical for both meals.
  • the composition and energy values of the ingredients used in each meal are presented in the table below.
  • Table 14 Composition and energy values of ingredients used to prepare the meals.
  • the total energy content of the meal prepared with the lamb hydrolysate as the meat source was 701.3 kilocalories of which 17 % was protein, 26 % was fat and 57 % was carbohydrate (36 g hydrolysate, 20 g canola oil and 100 maltodextrin).
  • the total energy content of the meal prepared with the casein as the meat source was 703.2 kilocalories of which 17 % was protein, 26 % was fat and 57 % was carbohydrate (33 g casein, 20 g canola oil and 100 maltodextrin).
  • the meals were isonitrogenous providing 320 mmol of nitrogen.
  • the volunteers were randomised into two groups; one group received the meat protein meal and the other received the casein protein meal. The subjects arrived at 0750 in a fasted state. Following baseline collections of blood and urine, the volunteers ingested the test meal. The study was performed while the participants were resting in a semi-recumbent position and no other food was ingested until the end of the study period. Water was given bi-hourly. Blood was collected from each subject every 30 minutes for three hours and then every hour for the following five hours. Blood was collected into Vacutainers with no anticoagulant (serum) or into Vacutainers containing oxalate/fluoride (plasma). Between blood draws the cannula was flushed with sterile physiological saline.
  • Serum samples were left to stand at room temperature for 30 minutes and plasma samples were immediately placed on ice. All samples were centrifuged for 10 minutes at 3 000 RPM at 4 °C, aliquoted and frozen within one hour of collection and stored at - 20 °C until processing. Total urine was collected every two hours throughout the eight hour period. Urine samples were stored at - 4 °C with thymol crystals and paraffin added as preservatives or were immediately frozen at - 20 °C depending on the chemical analysis.
  • Plasma glucose was measured using a hexokinase method.
  • Serum insulin was measured using a double antibody radioimmunoassay method.
  • Serum urea, urinary creatinine and urinary urea were assayed using an enzymatic method.
  • Urinary ammonia was measured using an enzymatic method using glutamate dehydrogenase.
  • urea and ammonia were isolated from urine on a Na + form of a cation exchange resin (Biorad Dowex AG50-X8, Sigma-Aldrich).
  • urine 7 ml was mixed with resin (2 ml) for 20 minutes. The supernatant was kept and the resin containing urinary ammonia was washed 5 times with distilled water. The supernatant (2 ml) was mixed with resin (2 ml) and incubated for 2 hours at 30 °C in the presence of urease (20 ⁇ ; Sigma- Aldrich). The resin containing urinary urea-derived ammonia was then washed with distilled water and stored at 4 °C for isotopic determination.
  • a cation exchange resin Biorad Dowex AG50-X8, Sigma-Aldrich
  • the serum proteins were precipitated by mixing serum (2 ml) with 5- sulpho-salicylic acid (Sigma-Aldrich). After centrifugation (2400 g, 25 min, 4 °C) the pellet containing the serum proteins was freeze-dried and stored until analysis. The supernatant was kept and buffered at pH 7. The urea was isolated from free amino acids on 2 ml of resin in the presence of urease (8 ⁇ ). After incubation for 2 hours at 30 D C the supernatant containing free amino acids was removed. The resin containing urea-derived ammonia from serum was washed with distilled water and stored at 4 °C.
  • Ntot was calculated as the product of the urinary urea nitrogen concentration and the volume of urine excreted.
  • N tot in the serum protein pool was determined as the serum concentration of protein nitrogen multiplied by the serum volume estimated to be 5 % of body weight (Ganong, 2005).
  • TBW was determined according to the equation of Watson et al. (1980).
  • Net postprandial protein utilization and postprandial biological value At the end of the 8 hour experimental period the amount of dietary nitrogen retained in the body or net postprandial protein utilization (NPPU; % of ingested nitrogen) was calculated as follows:
  • NPPU [Njngested — ⁇ N ex o-ileal ⁇ N e xo-urinary - ⁇ N exo- body urea (8h)] / Nj n g es te d
  • ⁇ N e x 0- iieai is the cumulative recovery over 8 h of dietary nitrogen collected in ileal digesta
  • ⁇ N exo -urinary is the cumulative recovery over 8 h of dietary nitrogen incorporated into urinary ammonia and urea
  • ⁇ N e x 0- body urea (8 h) is the dietary nitrogen incorporated into body urea at 8 h.
  • the postprandial biological value (PBV; % of ingested nitrogen) was calculated as the relative amount of dietary nitrogen absorbed that was not deaminated during the postprandial period:
  • AUC area under the curve
  • the areas under glucose and insulin curves were determined in Prism using the trapezoid rule. Differences in AUC between meals were then determined using two sample t-tests. Data are presented as means ⁇ standard error. A p value ⁇ 0.05 was considered to be statistically significant.
  • Table 15 Anthropometric measurements for study volunteers.
  • the serum insulin concentrations in older adult humans fed a mixed meal containing either 15 N-labelled lamb hydrolysate or casein are shown in Figure 10.
  • Dietary nitrogen incorporation into serum protein pools Time courses of isotopic 15 N concentration enrichments were measured in serum protein and urinary nitrogen pools which allowed for the quantification of dietary nitrogen in each pool. Dietary nitrogen incorporation into the serum protein pool was determined following the ingestion of the two 15 N-labelled meals and the results are shown in Figure 11. The incorporation of dietary nitrogen into the serum protein pool increased during the first 4 hours after the ingestion of the lamb hydrolysate meal reaching a maximum of 7.6 ⁇ 0.7 % at 8 hours. The incorporation of dietary nitrogen into the serum protein pool reached a plateau after 7 hours with 10.7 ⁇ 0.4 % of the ingested nitrogen from the casein meal present in the serum proteins 8 hours after meal ingestion. The amount of dietary nitrogen incorporated into the serum protein pool 8 hours after meal ingestion was significantly higher for the casein meal compared to the lamb hydrolysate meal (p ⁇ 0.05).
  • Dietary nitrogen deamination and urea production Dietary nitrogen incorporation into body urea (Figure 12) increased during the first 3 hours and reached a quasi-plateau from 3 to 5 hours following the ingestion of the lamb hydrolysate meal, peaking at 10.5 ⁇ 1.0 % of the ingested nitrogen and then declining slowly for the last three hours to 7.8 ⁇ 0.8 % of the ingested nitrogen. Dietary nitrogen from the casein meal was transferred to the body urea pool more slowly to reach a maximum of 8.3 ⁇ 1.3 % at four hours and then declined to 6.7 ⁇ 0.9 % of the ingested nitrogen at 8 hours.
  • the level of dietary nitrogen recovered in the body urea pool was not different between the two meals at 8 hours (p > 0.05).
  • the amount of dietary nitrogen excreted in the urine in the form of urea and ammonia was not different between the lamb hydrolysate and the casein meals at 8 hours (5.5 ⁇ 09 and 5.8 ⁇ 0.9 %, p > 0.05; 0.2 ⁇ 0.03 and 0.3 ⁇ 0.1 %, p > 0.05 respectively).
  • Total overall urea production was not different following the consumption of either meal with the rate of urea production being highest during the first four hours.
  • Urea production of direct dietary origin (B) was similar between the meals for the first six hours but was significantly less between 6 - 8 hours for the lamb hydrolysate meal (0.001 ⁇ 0.001 mmol N/kg body weight).
  • the endogenous urea production (C) was not different between the two meals over the 8 hour collection period.
  • the metabolic utilization of dietary nitrogen after the ingestion of the lamb hydrolysate meal was characterised by losses of dietary nitrogen not retained after 8 hours of 15.1 % (1.6 % ileal losses and 13.5 ⁇ 1.3 % deamination losses) and by a NPPU of 84.5 ⁇ 1.4 %.
  • the metabolic utilization of dietary nitrogen after the ingestion of the casein meal was characterised by losses of 18.9 % (5.9 % ileal losses and 13.0 ⁇ 1.3 % deamination losses) and by a NPPU of 74.8 ⁇ 1.3 %.
  • the NPPU of the lamb hydrolysate was significantly higher (p ⁇ 0.05) than that of casein.
  • Table 16 Comparison of bioavailability and postprandial metabolic utilization of, dietary nitrogen 8 h after ingestion of a single mixed meal containing hydrolyzed lamb protein or casein in older adult humans.
  • N and amino acids of dietary origin are submitted to sequential metabolic processes including gastrointestinal digestion and amino acid absorption, amino acid deamination, subsequent transfer to ammonia and urea or incorporation into organs. Labelling the dietary protein with 5 N made it possible to follow the metabolic fate of the dietary nitrogen and determine the postprandial nitrogen utilization of a lamb meat hydrolysate by measuring dietary nitrogen intake and absorption in older adults.
  • the digestive stage of protein utilization was previously determined in our laboratory using two animal models suitable for studying amino acid digestion. Rats and pigs are often used as models for determining true ileal digestibility of proteins.
  • the pig is a validated animal model for the determination of protein digestibility to the end of the small intestine for humans (Moughan & Rowan 1989, Rowan et al. 1994). It is appropriate to determine digestibility at the end of the small intestine because the digestion of protein and subsequent absorption of amino acids occur mainly in the upper small intestine and are effectively completed by the end of the ileum (Moughan et al. 2005).
  • the calculated true ileal digestibility of the lamb hydrolysate amounted to 97.2 ⁇ 1.1 using the rat model and 98.4 ⁇ 0.8% using the pig model. These values are high particularly when compared to the true ileal digestibility of milk and plant proteins demonstrating that the amino acids in the meat hydrolysate are absorbed almost completely anterior to the end of the small intestine.
  • TID True ileal digestibility of lamb meat hydrolysate determined in a rat model and a pig model
  • TID True ileal digestibility
  • PAV postprandial biological value
  • NPPU net postprandial protein utilization
  • NPPU is an appropriate measure of the nutritional value of a protein as it takes into account both bioavailability and the efficiency of the utilization of protein nitrogen. In this context the NPPU method allows for the discrimination of nutritional quality between proteins.
  • the NPPU for the lamb hydrolysate was 84.5 %.
  • the NPPU of both plant and milk proteins were lower than the meat hydrolysate (Table 18).
  • the difference in protein quality of 10.0 % between the lamb hydrolysate and casein was highly significant as this difference was not obvious when ileal digestibility or postprandial biological values were compared.
  • Bos C Airinei G, Mariotti F, Benamouzig R, Berot S, Evrard J, Fenart E, Tome D & Gaudichon C (2007).
  • the poor digestibility of rapeseed protein is balanced by its very high metabolic utilization in humans.

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Abstract

L'invention concerne un procédé de préparation d'une composition d'hydrolysat à partir d'une source de viande, qui consiste notamment : a) à hydrolyser au moins un type de protéine dans la source de viande, au moins partiellement du fait de l'utilisation d'au moins une protéase; b) à limiter le processus d'hydrolyse pendant une période de 2 à 5 heures par désactivation de la protéase pour former un mélange d'hydrolysat, se caractérisant par l'étape c) qui consiste à extraire la protéine à partir de la viande séparée mécaniquement.
PCT/NZ2012/000027 2011-03-04 2012-03-02 Procédé de fabrication d'une composition comestible WO2012121612A1 (fr)

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WO2015050294A1 (fr) 2013-10-04 2015-04-09 Innoway Co., Ltd Hydrolysat de protéine animale, son procédé de production et utilisation associée
JP2017513508A (ja) * 2014-04-28 2017-06-01 インターナショナル ディハイドレーティッド フーズ， インコーポレイテッド 小粒径のタンパク質組成物および製造方法

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Publication number Priority date Publication date Assignee Title
WO2015050294A1 (fr) 2013-10-04 2015-04-09 Innoway Co., Ltd Hydrolysat de protéine animale, son procédé de production et utilisation associée
EP3052641A1 (fr) * 2013-10-04 2016-08-10 Innoway Co. Ltd. Hydrolysat de protéine animale, son procédé de production et utilisation associée
EP3052641A4 (fr) * 2013-10-04 2017-04-05 Innoway Co. Ltd. Hydrolysat de protéine animale, son procédé de production et utilisation associée
JP2017513508A (ja) * 2014-04-28 2017-06-01 インターナショナル ディハイドレーティッド フーズ， インコーポレイテッド 小粒径のタンパク質組成物および製造方法
EP3136875A4 (fr) * 2014-04-28 2017-12-13 International Dehydrated Foods, Inc. Compositions de protéine de petite taille de particule et procédés de préparation
EP3906786A1 (fr) * 2014-04-28 2021-11-10 International Dehydrated Foods, Inc. Compositions de protéine de petite taille de particule et procédés de préparation

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