WO2015166312A1 - Méthode de production de collagène hydrolysé utilisant le nid d'hirondelle salangane comme matière première - Google Patents

Méthode de production de collagène hydrolysé utilisant le nid d'hirondelle salangane comme matière première Download PDF

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Publication number
WO2015166312A1
WO2015166312A1 PCT/IB2014/062056 IB2014062056W WO2015166312A1 WO 2015166312 A1 WO2015166312 A1 WO 2015166312A1 IB 2014062056 W IB2014062056 W IB 2014062056W WO 2015166312 A1 WO2015166312 A1 WO 2015166312A1
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WIPO (PCT)
Prior art keywords
solvent base
collagen
hydrolyzed collagen
nest
swiftlet
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Ceased
Application number
PCT/IB2014/062056
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English (en)
Inventor
Sk Sean SOO
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Individual
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Individual
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Publication date
Application filed by Individual filed Critical Individual
Priority to HK16106467.3A priority Critical patent/HK1218555B/zh
Priority to JP2016516298A priority patent/JP2016520609A/ja
Priority to PCT/IB2014/062056 priority patent/WO2015166312A1/fr
Priority to CN201480025618.1A priority patent/CN105377957B/zh
Publication of WO2015166312A1 publication Critical patent/WO2015166312A1/fr
Anticipated expiration legal-status Critical
Ceased legal-status Critical Current

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Classifications

    • C—CHEMISTRY; METALLURGY
    • C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
    • C08H—DERIVATIVES OF NATURAL MACROMOLECULAR COMPOUNDS
    • C08H1/00—Macromolecular products derived from proteins
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
    • A23L29/00—Foods or foodstuffs containing additives; Preparation or treatment thereof
    • A23L29/20—Foods or foodstuffs containing additives; Preparation or treatment thereof containing gelling or thickening agents
    • A23L29/275—Foods or foodstuffs containing additives; Preparation or treatment thereof containing gelling or thickening agents of animal origin, e.g. chitin
    • A23L29/281—Proteins, e.g. gelatin or collagen
    • A23L29/284—Gelatin; Collagen
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
    • 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
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P17/00—Drugs for dermatological disorders
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P17/00—Drugs for dermatological disorders
    • A61P17/02—Drugs for dermatological disorders for treating wounds, ulcers, burns, scars, keloids, or the like
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P19/00—Drugs for skeletal disorders
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P19/00—Drugs for skeletal disorders
    • A61P19/04—Drugs for skeletal disorders for non-specific disorders of the connective tissue
    • C—CHEMISTRY; METALLURGY
    • C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
    • C08L—COMPOSITIONS OF MACROMOLECULAR COMPOUNDS
    • C08L89/00—Compositions of proteins; Compositions of derivatives thereof
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
    • A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs

Definitions

  • Collagen is composed of a triple helix, which generally consists of two identical chains (al) and an additional chain that differs slightly in its chemical composition (a2).
  • the amino acid composition of collagen is atypical for proteins, particularly with respect to its high hydroxyproline content.
  • the most common motifs in the amino acid sequence of collagen are glycine-proline-X and glycine-X-hydroxyproline, where X is any amino acid other than glycine, proline or hydroxyproline.
  • Hydrolyzed collagen is a form of collagen. It is also called collagen hydrolysate, collagen peptide, gelatine, gelatine hydrolysate and hydrolyzed gelatine.
  • the amino acid content of hydrolyzed collagen is the same as collagen. It is water soluble and contains peptides like amino acids as well as glycine, proline, hydroxyproline, and glutamic acid, which help form new collagen in the body.
  • hydrolyzed collagen may be found in topical creams, acting as a product texture conditioner, and moisturizer.
  • the mechanism of action of ingested hydrolyzed collagen on skin may be the increased density of collagen fibrils and the fibroblasts' density (the fibroblasts being the main cells of the dermis, and those producing collagen). It may be that that the peptides of ingested hydrolyzed collagen have chemotactic properties on fibroblasts or an influence on growth of fibroblasts.
  • hydrolyzed collagen may promote lean muscle mass through the burning of fat rather than carbohydrates and proteins, toning and thickening skin, joint rebuilding, arterial strengthening, increased energy, organ rebuilding, alleviate osteoporosis, as well as lessening the symptoms of arthritis, high blood pressure, bladder weakness, chronic fatigue, shallow breathing, autoimmune, skin problems, and splitting nails.
  • Swiftlet are birds contained within the four genera Aerodramus, Hydrochous, Schoutedenapus and Collocalia. They form the Collocaliini tribe within the swift family Apodidae. The group contains around thirty species mostly confined to southern Asia, south Pacific islands, and northeastern Australia, all within the tropical and subtropical regions.
  • the bracket-shaped nest is white and translucent and is made of layers of hardened saliva attached to the rock.
  • Swiftlet nest has been used for centuries whether as a tonic or a health food. Consuming swiftlet nest regularly can give a person exuberant physical and mental strength as well as to restore one's youthfulness. The tonic power of swiftlet nest is believed to improve skin complexion and to slow the aging effect.
  • swiftlet nest has been traditionally prescribed to cure certain diseases for many generations, the actual characteristics and properties of swiftlet nest has not been thoroughly studied. Its usage and benefits are mainly based on historical, anecdotal and observational reports.
  • This invention is a breakthrough from tradition.
  • Swiftlet nest is cooked above 100°C, using steam sterilization method.
  • Amino acids analysis has been carried out on the sample of the swiftlet nest cooked using this invention. It shows the amino acids profile does fit the amino acids profile of collagen and hydrolyzed collagen.
  • swiftlet nest proved to be a source rich in amino acids and can be used as the raw material to produce collagen and hydrolyzed collagen.
  • Raw Material hydrolyzed collagen available in the market is produced from collagen found in the bones, skin, and connective tissue of animals such as cattle, fish, horses, pigs, and rabbits. All these are animal parts. Although only the by-products are used, this may raise concern to vegetarians and animal activists.
  • Non Organic The process of hydrolysis involves breaking down the molecular bonds between individual collagen strands using combinations of heat, acids, alkalis, or enzymes. Except if the process only involve heat alone, other methods involve the application of chemical components.
  • Hydrolyzed collagen refers to enzymatically or chemically processed collagen derived from marine life, though it can also be taken from bovine, ox, pig skin, and bone. Hydrolyzed collagen derived from bovine bone and cartilage involves having the bone crushed, ground, defatted, soaked in acid to remove the calcium, soaked again to break the collagen bonds and then dehydrated. This process results in small, intact amino acids which have not been damaged. These amino acids are quickly absorbed into the bloodstream, and are used as the building blocks of new collagen.
  • hydrolyzed collagen Another common means of producing hydrolyzed collagen are prolonged boiling in a strong acid (acid-HVP) or strong base or using an enzyme such as the pancreatic protease enzyme to simulate the naturally occurring hydrolytic process.
  • acid-HVP acid-HVP
  • pancreatic protease enzyme an enzyme such as the pancreatic protease enzyme to simulate the naturally occurring hydrolytic process.
  • hides are put in a lime slurry pit for up to 3 months, loosening collagen bonds; the hides are then washed to remove lime, and the collagen extracted in boiling water.
  • the extracted collagen is evaporator concentrated, desiccated with drum driers, and pulverized.
  • Hydrolyzed collagen like gelatin, is made from animal parts, including skin, bones, and connective tissue. It is possible that consumption of hydrolyzed collagen risks contraction of Transmissible spongiform encephalopathy.
  • Hydrolyzed collagen produced from the animal parts sources contains 8 out of 9 essential amino-acids, including glycine and arginine - two amino-acid precursors necessary for the biosynthesis of creatine. Glycine and proline concentration is as much as 20 times higher than other food sources of protein. However, it contains no tryptophan and is deficient in isoleucine, threonine, and methionine, all are essential amino acids, which means that humans cannot synthesize it, so it must be ingested.
  • swiftlet nest is full of protein. Due to traditional assumption that swiftlet nest should not be cooked at high temperature to avoid nutrition loss, swiftlet nest is therefore cooked using double steaming, also called double boiling, a Chinese cooking technique to prepare delicate food. This could be the reason that up to the present time, protein from swiftlet nest has not been widely studied and researched.
  • This invention bypasses orthodox assumption, by applying comtemporary cooking method, and discovered swiftlet nest is an alternative (if not better) source of amino acids, hence collagen and hydrolyzed collagen.
  • This invention introduce a production methodology which involves pre-cooking procedures and high temperature cooking procedures to produce hydrolyzed collagen from swiftlet nest.
  • Swiftlet nest is soaked in water for 8 hours, then drain dry. Once the soaking water is fully drained and replaced with solvent base, it is cooked using pressure cooking method. Total cooking time is about 1 hour.
  • Pressure cooking allows food to be cooked with greater humidity and higher temperatures than possible with conventional boiling or steaming methods.
  • the boiling point of water is 100 °C (212 °F) at standard pressure; the temperature of food is limited by the boiling point of water because excess heat causes boiling water to vaporize into steam.
  • the boiling point of water increases as the pressure rises, resulting in superheated water.
  • water in a pressure cooker can reach a temperature of up to 121 °C (250 °F), depending on altitude.
  • Botulism poisoining One of the major risk of canned/bottled food is botulism poisoining.
  • the poison is produced by Clostridium botulinum, a bacterium that is commonly found in soil, or on raw fruits and vegetables, on meat and fish and many others foods and surfaces. Botulism spores are tough, and cannot be killed with boiling water or heat without including canning pressures. 116°C is the minimum temperature necessary to destroy botulism spores, and the only way to guarantee safe canning for food items rich in protein such as meats and seafood.
  • Pressure cooking at a holding time of at least 15 minutes at 121 °C (250 °F) at 100 kPa (15 psi), or 3 minutes at 134 °C (273 °F) at 100 kPa (15 psi) will inactivate all fungi, bacteria, viruses and also bacterial spores, which can be quite resistant.
  • the contamination risk is reduced to the minimal as no additional steps are needed to transfer and pack the finished product.
  • tryptophan is absence, significant presence of threonine and isoleucine, with similar trace of methionine.

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  • Health & Medical Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Medicinal Chemistry (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Organic Chemistry (AREA)
  • Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
  • Polymers & Plastics (AREA)
  • General Chemical & Material Sciences (AREA)
  • Pharmacology & Pharmacy (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Animal Behavior & Ethology (AREA)
  • General Health & Medical Sciences (AREA)
  • Public Health (AREA)
  • Veterinary Medicine (AREA)
  • Dermatology (AREA)
  • Nutrition Science (AREA)
  • Physical Education & Sports Medicine (AREA)
  • Food Science & Technology (AREA)
  • Biomedical Technology (AREA)
  • Mycology (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Molecular Biology (AREA)
  • Biochemistry (AREA)
  • Materials Engineering (AREA)
  • Zoology (AREA)
  • Dispersion Chemistry (AREA)
  • Cosmetics (AREA)
  • Coloring Foods And Improving Nutritive Qualities (AREA)
  • Medicines Containing Material From Animals Or Micro-Organisms (AREA)
  • Medicinal Preparation (AREA)
  • Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)

Abstract

Les avantages en termes de santé démontrés par la consommation de collagène/collagène hydrolysé et de nid d'hirondelle salangane sont comparables. L'instinct logique aurait dû mettre en relation les deux concepts. Toutefois, du fait de croyances séculaires et de préjugés culturels, cette relation a été occultée. Le nid d'hirondelle salangane est consommé par la société chinoise comme un raffinement culinaire, un médicament efficace, ou encore un rehausseur de beauté. A tel point qu'il est devenu un aliment de classe vendu très cher. De ce fait, la culture selon laquelle "'ce qui n'est pas cassé ne nécessite pas réparation" s'est diffusée. La méthode de cuisson dite double cuisson à la vapeur, parfois appelée double bain-marie, est la seule méthode qui s'est imposée jusqu'à nos jours. Elle est fondée sur la croyance selon laquelle une cuisson excessive au-delà de 100°C détruit la valeur nutritive du nid d'hirondelle salangane. Cette invention est une avancée par rapport à la tradition. Le nid d'hirondelle salangane est cuit à plus de 100°C par un procédé de stérilisation à la vapeur. Une analyse des acides aminés a été effectuée sur l'échantillon de nid d'hirondelle salangane cuit selon le procédé de l'invention. Elle montre que le profil des acides aminés correspond à celui des acides aminés du collagène et du collagène hydrolysé. Ainsi, avec la présente invention, le nid d'hirondelle salangane s'est avéré être une source riche en acides aminés qui peut être utilisée comme matière première pour produire du collagène et du collagène hydrolysé.
PCT/IB2014/062056 2014-06-08 2014-06-08 Méthode de production de collagène hydrolysé utilisant le nid d'hirondelle salangane comme matière première Ceased WO2015166312A1 (fr)

Priority Applications (4)

Application Number Priority Date Filing Date Title
HK16106467.3A HK1218555B (zh) 2014-06-08 使用金丝燕窝作为原料生产水解胶原蛋白的方法
JP2016516298A JP2016520609A (ja) 2014-06-08 2014-06-08 アナツバメの巣を原材料とする加水分解コラーゲンの製造法
PCT/IB2014/062056 WO2015166312A1 (fr) 2014-06-08 2014-06-08 Méthode de production de collagène hydrolysé utilisant le nid d'hirondelle salangane comme matière première
CN201480025618.1A CN105377957B (zh) 2014-06-08 2014-06-08 使用金丝燕窝作为原料生产水解胶原蛋白的方法

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
PCT/IB2014/062056 WO2015166312A1 (fr) 2014-06-08 2014-06-08 Méthode de production de collagène hydrolysé utilisant le nid d'hirondelle salangane comme matière première

Publications (1)

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WO2015166312A1 true WO2015166312A1 (fr) 2015-11-05

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PCT/IB2014/062056 Ceased WO2015166312A1 (fr) 2014-06-08 2014-06-08 Méthode de production de collagène hydrolysé utilisant le nid d'hirondelle salangane comme matière première

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JP (1) JP2016520609A (fr)
CN (1) CN105377957B (fr)
WO (1) WO2015166312A1 (fr)

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Publication number Priority date Publication date Assignee Title
CN109123638A (zh) * 2018-09-13 2019-01-04 海南众康养生科技有限公司 一种燕窝含片及其制备方法
CN112244284A (zh) * 2020-10-16 2021-01-22 大洲新燕(厦门)生物科技有限公司 一种阿胶爆趣珠燕窝及其制备方法

Citations (3)

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Publication number Priority date Publication date Assignee Title
JP2006223266A (ja) * 2005-02-21 2006-08-31 Jasmine:Kk 燕の巣の水煮を含有する栄養補給食品
CN102102119A (zh) * 2010-12-03 2011-06-22 北京中生奥普寡肽技术研究所 燕窝寡肽组合物及其制备方法和使用
WO2012006742A1 (fr) * 2010-07-16 2012-01-19 Justbio Inc. Procédé d'extraction permettant d'obtenir un extrait de stevia rebaudiana organique certifiable

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JP4020284B2 (ja) * 1999-05-27 2007-12-12 株式会社マンダム 育毛剤原料及び育毛剤組成物
CN101999654B (zh) * 2010-10-27 2012-11-28 大连海晏堂生物有限公司 一种燕窝膏食品的制作方法

Patent Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2006223266A (ja) * 2005-02-21 2006-08-31 Jasmine:Kk 燕の巣の水煮を含有する栄養補給食品
WO2012006742A1 (fr) * 2010-07-16 2012-01-19 Justbio Inc. Procédé d'extraction permettant d'obtenir un extrait de stevia rebaudiana organique certifiable
CN102102119A (zh) * 2010-12-03 2011-06-22 北京中生奥普寡肽技术研究所 燕窝寡肽组合物及其制备方法和使用

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HOUDRET N ET AL: "Purification and chemical study of a Collocalia glycoprotein", BIOCHIMIE 1975, vol. 57, no. 5, 1975, pages 603 - 608, XP002735128, ISSN: 0300-9084 *
HOWE C ET AL: "Collocalia mucoid: A substrate for myxovirus neuraminidase", ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, ACADEMIC PRESS, US, vol. 95, no. 3, 1 December 1961 (1961-12-01), pages 512 - 520, XP024813023, ISSN: 0003-9861, [retrieved on 19611201], DOI: 10.1016/0003-9861(61)90184-9 *
ROUTRAY WINNY ET AL: "Chemical Constituents and Post-Harvest Prospects of Pandanus amaryllifolius Leaves: A Review", FOOD REVIEWS INTERNATIONAL, TAYLOR & FRANCIS, PHILADELPHIA, USA, vol. 26, no. 3, 1 January 2010 (2010-01-01), pages 230 - 245, XP009147762, ISSN: 8755-9129, DOI: 10.1080/87559129.2010.484114 *

Also Published As

Publication number Publication date
CN105377957A (zh) 2016-03-02
JP2016520609A (ja) 2016-07-14
CN105377957B (zh) 2019-01-18
HK1218555A1 (zh) 2017-02-24

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