WO2012121613A2 - Utilisation d'une composition comestible - Google Patents

Utilisation d'une composition comestible Download PDF

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Publication number
WO2012121613A2
WO2012121613A2 PCT/NZ2012/000028 NZ2012000028W WO2012121613A2 WO 2012121613 A2 WO2012121613 A2 WO 2012121613A2 NZ 2012000028 W NZ2012000028 W NZ 2012000028W WO 2012121613 A2 WO2012121613 A2 WO 2012121613A2
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hydrolysate
protein
meat
hydrolysate composition
animal
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PCT/NZ2012/000028
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English (en)
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WO2012121613A3 (fr
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 WO2012121613A2 publication Critical patent/WO2012121613A2/fr
Publication of WO2012121613A3 publication Critical patent/WO2012121613A3/fr

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    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/01—Hydrolysed proteins; Derivatives thereof
    • A61K38/012—Hydrolysed proteins; Derivatives thereof from animals

Definitions

  • This invention relates to the use(s) of an edible composition.
  • BACKGROUND ART The present invention relates particularly to edible compositions in the form of hydroiysates which are hydrolysed biomatter typically prepared into compositions for human consumption.
  • Hydroiysates 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 hydroiysates stems from the compositions containing nutrients that can aid the recovery, maintenance and improvement of human health.
  • hydroiysates 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 e.g. amino acids
  • the nutrients available from these sources often do not effectively match the nutrient requirements of the human body. This is particularly so in the case of elderly people who have high requirements for amino acids.
  • a large amount 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.
  • 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.
  • many hydrolysates can have undesirable flavour profiles. Often the flavour level can be overbearingly salty or bitter, or the hydrolysate is bland.
  • 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. In many countries, 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 mistrust in meat quality can make commercialization non-viable. Therefore, it is critical to identify a source, be it animal or non-animal, 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). Absorption 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 in 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 all 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.
  • hydrolysate composition isolated from a meat source and containing 60 - 90% w/w protein, in the manufacture of a medicament, to treat amino acid malnourishment or an associated condition in an animal.
  • a method of treating an amino acid malnourishment or an associated condition in an animal using a hydrolysate composition wherein the hydrolysate composition is isolated from a meat source and the hydrolysate composition contains 60-90% w/w protein.
  • the hydrolysate composition is provided in a form wherein in the order of 30 g of protein can be consumed in a single time added into any serving size of food material.
  • a method of using a hydrolysate composition isolated from a meat source and containing 60 - 90 % w/w protein, characterised by the step of providing the hydrolysate composition in a nutritional supplement to an animal.
  • a method of using a hydrolysate composition wherein the hydrolysate composition is isolated from a meat source and containing 60 - 90 % w/w protein; characterised by the step of providing the hydrolysate composition in a medicament for the treatment of an amino acid malnourishment or an associated condition in an animal.
  • hydrolysate composition isolated from a meat source and containing 60 - 90% w/w protein, for the treatment of amino acid malnourishment or an associated condition in an animal.
  • a method of improving flavouring of a food stuff characterised by the step of adding to the food stuff a hydrolysate composition wherein the hydrolysate composition is isolated from a meat source and; wherein the hydrolysate composition contains 60 - 90% w/w protein.
  • 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 utilisation. The latter is determined by digestion and absorption processes in the small intestine.
  • the digestion and absorption processes are affected by many factors which include 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 concern because 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 nutritional supplement is geared at boosting health, promoting muscle growth and enhancing wellbeing.
  • the present hydrolysate could be used for body builders, athletes and individuals with special requirements like the elderly and pregnant woman.
  • amino acid malnourishment should be taken as meaning any disease or condition in the animal body which leads to a lower than acceptable level of at least one amino acid used in a human or other animal.
  • the amino acid malnourishment or an associated disorder may more easily affect the people with reduced immunity like those suffering from cancer, conditions associated with elderly population, starvation or poor diet in impoverished countries, AIDS patients, or post operative patients.
  • the composition or medicament of the present invention is provided in a soup, savory snack, cereal bar, drink, or any other form of food or nutraceutical easily consumed by the human or other animal.
  • alternative forms of delivery could be provided including a bolus or injectable material.
  • a novel feature of the hydrolysate is that it includes a protein level of between 60 and 90 % w/w.
  • the inventors have identified many sources from meat which are able to provide this level of protein for human consumption.
  • the meat source is mechanically separated (MS) meat from lamb, however the source of meat is not restricted to MS meat, nor just lamb and can include any form of meat.
  • MS meat is generally not used for consumption by humans because of its poor flavour and texture characteristics can be utilized to produce a protein hydrolysate which has superior flavour profile and is rich in amino acids.
  • the current invention thus helps to provide added value to the MS meat (e.g. the inventors have found they may convert a by-product costing 80 cents/kg MS meat into a product which may be sold for $25/kg hydrolysate)
  • different meat sources may be used, such as cattle or sheep.
  • 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 to be treated.
  • the hydrolysate of the present invention may still maintain a high protein level (60-90%), however subtle differences in amino acid balance may be altered to suit different needs by using different meat sources.
  • amino acid profile of the resulting hydrolysate may be well matched to the requirements of human growth and development, and overall well being e.g. vegetable sources like cereals are deficient in sulphur containing amino acids.
  • Other types of hydrolysates e.g. those from vegetable sources may have high levels of proteins upwards of 90% w/w.
  • the amino acid profile may not be well balanced to match the requirements of humans and other animals.
  • the essential amino acids are included in our diet. If the recipient is malnourished and is not receiving adequate amounts of these essential amino acids, many complications can arise. As such, the present hydrolysate may provide these essential amino acids in appropriate amounts, which may prevent or treat the complications. This is why an animal e.g. meat source is particularly advantageous over non-meat sources like vegetable sources of protein hydrolysates. Absorption/Digestability A further important feature of a hydrolysate is its level of absorption and digestibility.
  • Protein hydrolysates typically have undergone enzymatic digestion of the protein from the sourced material.
  • the hydrolysate of the present invention preferably has undergone extensive hydrolysis such that the average polypeptide is only two amino acids in length (discussed further in the best modes). This helps to ensure that the hydrolysate may be highly absorbed after consumption.
  • having a highly absorbable hydrolysate may be particularly advantageous.
  • the inventors consider it may be particularly advantageous to have highly hydrolysed protein in the hydrolysate. This means that a large percentage of the peptide links are severed by the hydrolysis to result in a mixture of small peptides or individual amino acids.
  • the inventors consider it may be beneficial to: have more than 40% digestion of the peptide links in the hydrolysate, have a high proportion of di- or tri- peptides or single amino acids in the hydrolysate, have approximately 78% or more of the peptides, which are less than 10 amino acids in length and/or have the average size of the peptide to be two amino acids in length.
  • the inventors have found that the hydrolysate from a meat source in accordance with the present invention is highly absorbed in the gastrointestinal track of pigs and mice. Studies showed that the true ileal digestibility is up to 98%. Furthermore, each type of amino acid is highly absorbable ensuring that each type of amino acid is effectively utilized by the human body. The inventors expect similar results in other animals including humans. The absorption of individual amino acids is highly dependent on the protein source. For example, the digestibility of many amino acids in humans differs between soy and milk proteins, and even between individual milk proteins, for example beta- lactoglobulin and casein.
  • the true llial digestibilities for different protein sources studied include, 94.1% for Casein, 91.5 % for soy, 95% for milk protein (casein and whey proteins), 92.3% for casein hydrolysate, where as the true ilial digestibility for lamb protein hydrolysate in accordance with the present invention was found to be 98.4%.
  • the high digestible amino acid content indicates that the hydrolysate of the present invention is an amino acid source high in valuable lysine.
  • This hydrolysate may have particular application to humans consuming diets high in cereals, for which lysine is often the first limiting amino acid. It may also be important for humans with muscle atrophy, such as the elderly or those undergoing rehabilitation after surgery or for athletes aiming to increase muscle mass.
  • the inventor's data also indicates that the absorption level of the present hydrolysate sourced from MS meat is exceptionally better than hydrolysates sourced from vegetable sources.
  • hydrolysates currently available can have a relatively high level of fat. This can often be due to difficulty in removing the fats from the protein source.
  • the present invention is particularly advantageous as the fats may be effectively removed without losing the good palatability characteristics of the meat hydrolysate.
  • the fats may be selectively removed while maintaining a high protein level and an excellent amino acid profile.
  • Hydrolysates sourced from vegetable sources for example are claimed to be high in protein content, low in fat content, and be palatable - similar to the features in the present invention.
  • a disadvantage of hydrolysates sourced vegetable sources is they do not have an amino acid profile that closely matches human requirements, i.e. meat.
  • some of the advantages and uses of the hydrolysate include:
  • the preferred hydrolysate sourced from NZ meat is a verified source of protein (e.g. body builders or infant formulators); represents a natural and/or organic supplement; - the ability to differentiate the product from those of competitors (e.g. by providing a "functional soup").
  • Figure 8 Odour intensity of the powders stored at the four temperatures over a period of 24 weeks in the category scale from 1 worst, to 10 neutral
  • B Taste intensity of agueous solutions each containing 2.1% of the powder in the category scale from 1 worst, to 10 neutral.
  • the powder samples were stored at the four temperatures over a period of 24 weeks.
  • Figure 9 Plasma glucose concentrations after the ingestion of a mixed meal containing 15 N-labelled lamb hydrolysate or casein in older adult humans;
  • Figure 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 can be 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 degree of hydrolysis in the order of 40%. 90% of the protein in the hydrolysate has a molecular weight of less than 1000 Daltons. Furthermore, 90% 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. However this should not be considered limiting - the applicant acknowledges that 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.
  • EXAMPLE 2 Method of Preparing the Hydrolysate
  • 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 equipments 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.
  • 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.
  • the hydrolysate liquor was concentrated using a rising film evaporator to a solids content of 30-40% under an exit temperature of 60°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. x 100
  • 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.
  • 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 depending on the storage time and temperature.
  • MS lamb meat and Meat hydrolysate 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: -20°C (control), 4°C, 20°C (room temperature) and 37°C over a period of 24 weeks. At regular 4 weekly intervals, four pouches were randomly removed from each of the storage rooms and evaluated for a range of physico-chemical and sensory measures.
  • 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.
  • a modified AOAC (950.81 ) method was used for water solubility measurement. Approximately 1 g of 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. Plate count test
  • 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).
  • 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/1 OOg of Meat hydroiysate assuming all the chloride (1.6g/1 OOg) was bound to sodium.
  • the table below shows the amino acid contents of Meat hydroiysate 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 hydroiysate than in the lamb leg muscle.
  • the methionine was 35% lower in Meat hydroiysate and the valine and histidine contents, on the other hand, were 10% higher in Meat hydroiysate than the lamb leg muscle.
  • the threonine, proline, glycine and methionine levels were about 10% lower in Meat hydroiysate than in raw meat.
  • the glutamic acid, valine and lysine levels in Meat hydroiysate were about 10% greater than in the raw MS lamb meat.
  • the hydroxyproline content in Meat hydroiysate 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 hydroiysate has a low collagen level.
  • 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 probably has 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.
  • 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 11.8 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 peaks at 15.3 min, 17.8 min and 20.1 min decreased in height with rising storage temperatures as shown in Figure 6. It would appear that both, the number of peaks and height of peaks in the
  • 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 numbers 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).
  • microbial quality was not an issue for this product. Effects of storage on tastes/odours of the product
  • Table 13 Plate counts of Meat hydrolysate stored at four temperatures for a
  • Meat hydrolysate contained 0.4% fat and 83.4% crude protein
  • 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
  • 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.
  • 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.
  • the purpose of this project was to evaluate the quality of a hydrolysed meat protein in older adult subjects by measuring its nitrogen utilization in the human body.
  • Lamb meat was enriched with 15nitrogen (or 15N), the stable isotope of nitrogen and the meat hydrolysed into a powder, incorporated into a meal as the sole source of protein and fed to participants.
  • Blood and urine samples were collected for 8 hours following the meal and analyses of these samples determined how much nitrogen from the meat hydrolysate was transferred into the body's nitrogen pool and excreted in the urine.
  • 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.
  • 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 lamb protein, uniformly and intrinsically labelled with 15 N.
  • the source of protein was either lamb 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.
  • 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 °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. Before isotopic determination resins were eluted with KHS0 4 (2.5 mol/L).
  • the 15 N: 14 N isotope ratio was determined by isotope-ratio mass spectrometry (Stable Isotopes Laboratory, GNS Science) in the urinary urea and ammonia, serum protein, free nitrogen and urea.
  • 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
  • NPPU [Ningested - ⁇ N eX o-ileal ⁇ ⁇ N e xo -urinary " ⁇ N exo -body urea (8h)] / Ni nges ted where ⁇ N e x 0 -iieai is the cumulative recovery over 8 h of dietary nitrogen collected in ileal digesta, ⁇ N ex0 -urinary is the cumulative recovery over 8 h of dietary nitrogen incorporated into urinary ammonia and urea and ⁇ N exo-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.
  • the anthropometric measurements for study participants are provided in the table below. There were no statistically significant differences among subjects fed either of the two test meals for any of the measured characteristics.
  • the plasma glucose concentrations increased significantly after ingestion of both meals and peaked at 30 minutes postprandially (7.0 ⁇ 0.2 and 6.6 ⁇ 0.6 mmol/L for the lamb hydrolysate and casein meals respectively). There were no significant differences in overall glucose concentrations, peak glucose concentrations or the AUC between the two meals (p > 0.05).
  • 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).
  • 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 15 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.
  • ⁇ SE True ileal digestibility
  • 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 Juillet B, Fouillet HL, Turlan L, Dare S, Luengo C, N ounda R, Benamouzig R, Gausseres N, Tome D et al. (2005). Postprandial metabolic utilization of wheat protein in humans.
  • Nutrition Research Reviews 2 161-180 Nutrition Research Reviews 2 161-180
  • Mariotti F Pueyo ME, Tome D, Berot S, Benamouzig R & Mahe S (2001 ). The influence of the albumin fraction on the bioavailability and postprandial utilization of pea protein given selectively to humans. Journal of Nutrition 131 1706-1713. Mariotti F, Pueyo ME, Tome D & Mahe S (2002). The bioavailability and postprandial utilization of sweet lupin (Lupinus albus)-flour protein is similar to that of purified soyabean protein in human subjects: a study using intrinsically N-15- labelled proteins. British Journal of Nutrition 87 315-323.

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Abstract

La présente invention concerne l'utilisation d'une composition d'hydrolysat isolée d'une source carnée et contenant 60 à 90 % en poids de protéine, dans la fabrication d'un médicament, afin de traiter une carence en acides aminés ou une pathologie associée chez un animal.
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Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
GB804293A (en) * 1956-03-22 1958-11-12 Simon Lyon Ruskin Improvements in or relating to the production of flavoured food compositions
US4452888A (en) * 1980-07-10 1984-06-05 Terumo Corporation Process for producing a low-molecular weight peptide composition and nutrient agent containing the same
US4853231A (en) * 1986-04-29 1989-08-01 Kazuharu Osajima Method for preparation of tastable matters consisting primarily of low molecular weight peptides
WO1994001003A1 (fr) * 1992-07-03 1994-01-20 Novo Nordisk A/S Procede de production d'un hydrolysat carne, et application de celui-ci
EP0611261B1 (fr) * 1993-02-02 2003-01-15 Italo Visaggio Composition nutritive pour personnes qui ne tolèrent pas le lait de vache et les protéines de soja et/ou le lactose

Patent Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
GB804293A (en) * 1956-03-22 1958-11-12 Simon Lyon Ruskin Improvements in or relating to the production of flavoured food compositions
US4452888A (en) * 1980-07-10 1984-06-05 Terumo Corporation Process for producing a low-molecular weight peptide composition and nutrient agent containing the same
US4853231A (en) * 1986-04-29 1989-08-01 Kazuharu Osajima Method for preparation of tastable matters consisting primarily of low molecular weight peptides
WO1994001003A1 (fr) * 1992-07-03 1994-01-20 Novo Nordisk A/S Procede de production d'un hydrolysat carne, et application de celui-ci
EP0611261B1 (fr) * 1993-02-02 2003-01-15 Italo Visaggio Composition nutritive pour personnes qui ne tolèrent pas le lait de vache et les protéines de soja et/ou le lactose

Non-Patent Citations (8)

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Title
BOZA J. ET AL.: 'Protein hydrolysate vs free amino acid-based diets on the nutritional recovery of the starved rat' EUR J NUTR vol. 39, 2000, pages 237 - 243 *
CLEMENTE A: 'Enzymatic protein hydrolysates in human nutrition' TRENDS IN FOOD SCIENCE & TECHNOLOGY vol. 11, 2000, pages 254 - 262 *
KUROZAWA L ET AL.: 'Effect of carrier agents on the physicochemical properties of a spray dried chicken meat protein hydrolysate' JOURNAL OF FOOD ENGINEERING vol. 94, 2009, pages 326 - 333 *
MANNINEN A: 'Protein Hydrolysates in Sports Nutrition' NUTRITION & METABOLISM vol. 6, no. 1, 28 September 2009, page 38 *
PELLET P ET AL.: 'Evaluation of the use of amino acid composition data in assessing the protein quality of meat and poultry products' THE AMERICAN JOURNAL OF CLINICAL NUTRITION vol. 40, September 1984, pages 718 - 736 *
ROSSI DM ET AL.: 'Biological evaluation of mechanically deboned chicken meat hydrolysate' REV. NUTR. vol. 22, no. 6, 2009, pages 879 - 885 *
VARAVINIT S ET AL.: 'Production of Meat-like Flavor' SCIENCEASIA 2000, pages 219 - 224 *
WEISELBERG B. ET AL.: 'A lamb-meat-based formula for infants allergic to casein hydrolysate formulas' CLIN PEDIATR (PHILA) vol. 35, no. 10, October 1996, pages 491 - 5 *

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