WO2012121611A2 - Composition comestible et son procédé de fabrication - Google Patents

Composition comestible et son procédé de fabrication Download PDF

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Publication number
WO2012121611A2
WO2012121611A2 PCT/NZ2012/000026 NZ2012000026W WO2012121611A2 WO 2012121611 A2 WO2012121611 A2 WO 2012121611A2 NZ 2012000026 W NZ2012000026 W NZ 2012000026W WO 2012121611 A2 WO2012121611 A2 WO 2012121611A2
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Prior art keywords
hydrolysate
meat
protein
lamb
nitrogen
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WO2012121611A3 (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 Ltd
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MEAT BIOLOGICS RESEARCH Ltd
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Publication of WO2012121611A3 publication Critical patent/WO2012121611A3/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 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

Definitions

  • 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, 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 leads to an increase in the cost of the product for the end- consumer.
  • 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, be it animal or non-animal, that not only has stringent regulatory approval, but also has consumer confidence.
  • 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. 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 un-wanted components. This can take up valuable time, equipment and/or can lead to a reduction of nutrients lost during the additional hydrolysis step.
  • hydroiysate composition isolated from a meat source characterized in that the hydroiysate 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 utilization. The latter is determined by digestion and absorption processes in the small intestine.
  • Lean red meats are acknowledged as being sources of superior quality protein and important micronutrients that are essential for good health throughout life. As we age, the ability to eat and digest proteins such as those contained in red meat 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 a special problem because protein-energy malnutrition is correlated with a higher rate of mortality and morbidity.
  • hydrolysate should be taken as meaning any biological material that has been hydrolysed or otherwise broken down, digested or cleaved, either enzymatically or non-enzymatically, into smaller components than normally present in the un-modified state of the starting biological material.
  • 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.
  • Providing the hydrolysate in a dry powder or soup mix may help to increase the shelf life, reduce space requirements during storage, and the need to refrigerate the composition. Indeed, studies performed by the inventors suggested the hydrolysate stored at room temperature was very stable over a temperature range between -20°C and 37°C over a 24 week trial period.
  • meat source should be taken as meaning any resource that contains proteins.
  • 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.
  • nutrients e.g. amino acid profile
  • hydrolysed lamb meat very closely matches the human muscle amino acid profile.
  • meat sources such as cattle, sheep, poultry and pigs can also be used.
  • the meat source is derived from mechanically separated (MS) meat.
  • the meat source is meat off cuts or offal.
  • the source is not restricted to these and can also include any form of meat.
  • a further advantage of using MS meat or off cuts is that the hydrolysate may utilise by-products that would otherwise be discarded. This may help to reduce costs in sourcing the meat used for the hydrolysate, or potentially even free. Additionally, providing a use for off-cuts may help to boost the profitability of the meat industry in New Zealand and other countries.
  • a protein range of 60%-90% w/w is what the preferred source (mechanically separated lamb meat) will most often provide using the preferred method outlined in the Best Modes section of this patent specification.
  • the novel range of protein in the present invention has many advantages over the prior art. For example, a high protein hydrolysate may be particularly beneficial to those who:
  • the preferred hydrolysates of the present invention include an appropriate balance of amino acids, including the essential amino acids.
  • the protein is rich in sulphur-containing amino acids, namely cysteine and methionine.
  • the current invention is not only rich in protein content having essential amino acids and has high digestibility, but also has an acceptable taste and does not require use of any additives or flavours to mask or alter the flavour profile of the product.
  • EXAMPLE 1 A description of the preferred hydrolysate of the present invention.
  • the hydrolysate is provided in a dry soup mix or powder.
  • 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 2 List of equipments used in manufacture of hydrolysate powder from MS lamb meat
  • 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.
  • the hydrolysate liquor was concentrated using a rising film evaporator to a solids content of 30-40% under an exit temperature of 60°C.
  • the obtained hydrolysate powder is finally packaged in aluminum foil bags under vacuum and stored at -20°C.
  • CFU Colony Forming Unit
  • 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
  • MS lamb meat was purchased from PPCS's plant, Oringi, New Zealand. Meat hydrolysate was produced and spray-dried by New Zealand Pharmaceuticals Ltd. (NZP) according to a protocol that was developed by the Riddet Centre of Massey University, Palmerston North.
  • 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.
  • 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
  • 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.
  • 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 Composition (g/100g) of IV eat hydrolysate:
  • 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.
  • 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 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 sample stored at 20°C produced a peak (93,000 au) at an elution time of 3.3 min, giving an additional character feature to the sample, which made up 32.6% of its total components. These changes are also evidence pointing to a loss of flavour components with increase in storage temperature.
  • 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.
  • 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
  • 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.
  • Colour spaces of all the powder samples stored at the four temperatures for a 24 week period changed with time within a narrow range, L * changing by 2.2% from 61.5 to 62.9, a* by 3.6% from 5.85 to 6.06 and b * by 7.6% from 13.43 to 4.53.
  • the samples stored at 20°C and particularly 37°C showed greater colour changes with time than the samples stored at 4°C or less.
  • 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 results indicate a very high degree of amino acid utilization of the lamb meat hydrolysate amino acids, when they were fed to human subjects in the form of a soup.
  • 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 were recruited from the Palmerston North area through advertisements in the local media and selection from the electoral role. 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.
  • 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 labeled 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 iso-nitrogenous providing 320 mmol of nitrogen.
  • the volunteers were randomized 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.
  • urea and ammonia were isolated from urine on a Na + form of a cation exchange resin (Biorad Dowex AG50-X8, Sigma-Aldrich, Auckland, NZ).
  • a cation exchange resin Biorad Dowex AG50-X8, Sigma-Aldrich, Auckland, NZ.
  • 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, Auckland, NZ).
  • the resin containing urinary urea- derived ammonia was then washed with distilled water and stored at 4 °C for isotopic determination.
  • serum urea extraction the serum proteins were precipitated by mixing serum (2 ml) with 5-sulpho-salicylic acid (Sigma-Aldrich, Auckland, NZ). 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.
  • N to t 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).
  • the nitrogen in the body urea pool was calculated assuming that urea was uniformly distributed throughout the total body water (TBW) and according to the following equation:
  • Nbody urea C urea X TBW / 0.92
  • C urea is the urea nitrogen concentration in the serum sample at the collection time and 0.92 is the correction factor for the water content of serum.
  • 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:
  • 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 in older adult humans fed a mixed meal containing either 5 N-labelled lamb hydrolysate or casein are shown in Figure 9.
  • 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 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 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).
  • nitrogen 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 1 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 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.
  • 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 considerably less (Table 16). 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.

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Abstract

La présente invention concerne une composition d'hydrolysat isolée d'une source carnée. La composition est caractérisée en ce que l'hydrolysat contient 60 à 90 % en poids de protéine dont le taux d'humidité est inférieur à 20 %.
PCT/NZ2012/000026 2011-03-04 2012-03-02 Composition comestible et son procédé de fabrication Ceased WO2012121611A2 (fr)

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* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
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
CA1198072A (fr) * 1982-02-22 1985-12-17 Nicholas Melachouris Procede de preparation d'hydrolysate de proteines
DK87692D0 (fr) * 1992-07-03 1992-07-03 Novo Nordisk As
DK46793D0 (da) * 1993-04-26 1993-04-26 Novo Nordisk As Enzym

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