• Food Science of Animal Resources
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• v.36 no.4
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• pp.516-522
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• 2016

Goat milk is highly nutritious and is consumed in many countries, but the development of functional foods from goat milk has been slow compared to that for other types of milk. The aim of this study was to develop a goat milk protein hydrolysate (GMPH) with enhanced digestibility and better hypoallergenic properties in comparison with other protein sources such as ovalbumin and soy protein. Goat milk protein was digested with four commercial food-grade proteases (separately) under various conditions to achieve the best hydrolysis of α_s -casein and β-lactoglobulin. It was shown that treatment with alcalase (0.4%, 60℃ for 30 min) effectively degraded these two proteins, as determined by SDS-PAGE, measurement of nonprotein nitrogen content, and reverse-phase high-performance liquid chromatography. Hydrolysis with alcalase resulted in a significant decrease in β-lactoglobulin concentration (almost to nil) and a ~40% reduction in the level of α_s-casein. Quantification of histamine and TNF-α released from HMC-1 cells (human mast cell line) showed that the GMPH did not induce an allergic response when compared to the control. Hence, the GMPH may be useful for development of novel foods for infants, the elderly, and convalescent patients, to replace cow milk.

• Korean journal of food and cookery science
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• v.7 no.4
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• pp.93-101
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• 1991

The object of this study was to investigate characteristics of kiwifruit protesae and effect of this enzyme on the functionality of casein. The specific activity of crudely prepared kiwifruit pretense on casein was 196.95 units/mg protein, it showed optimum activity at pH 3.0, $60^{\circ}C$. The degree of hydrolysis of casein with pretense treatment steeply increased to 73.5% and 78.9% for 10 and 20 minutes and then reached 84.1% and 89.3% for 1 and 4 hours, respectively. Solubility of non heated control group was 0.2% at pH 4, while the sample groups treated with enzyme for 0, 10 and 20 minutes were 14.5%, 19.2% and 24.0%, respectively. Casein treated with pretense showed marked increase in foam expansion near isoelectric point. However, enzymatically treated groups had lower foam expansion than the control groups. Foam stabilities of enzymatically modified group were lower than those of the control groups at all pH. Emulsifying activity of the non-heated control group was 0% at pH 4, while the groups modified enzymatically for 0, 10, and 60 minutes showed 51.0%, 55.5% and 54.5%, respectively.

• Food Science of Animal Resources
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• v.41 no.4
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• pp.687-700
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• 2021

This study performed to evaluate the applicability of functional dairy food materials by comparing the calcium solubilization ability and anti-inflammatory effects of hydrolyzed casein protein. Commercial enzyme (Alcalase^®; Neutrase^®; Protamex^®; Flavourzyme^®) was added to the 10% casein solution to prepare the casein hydrolysates. Samples obtained every hour [1:200 (w/v)]. According to results of measuring the degree of hydrolysis (DH), all of four enzymatic hydrolysates increased rapidly from 30 to 40 min, and after 150 min, there were no change. Protamex^® and Neutrase^® had the highest DH compared to others enzymatic hydrolysates. After that, peptides obtained throughout a preparative liquid chromatography system. In the calcium solubility experiments, neutrase fraction (NF) 4 and NF7 showed similar activities with casein phosphopeptide (CPP). In vitro cell experiments showed that no cytotoxicity except for NF6. Also, the production of nitric oxide (NO) inhibited as the concentration of fraction samples increased. The cytokine (IL-1α, IL-6, and TNF-α) production was lower than lipopolysaccharide (+) group significantly. Therefore, the possibility of anti-inflammatory activity found in the hydrolyzed samples. According to the above experiments, NF3 and Protamex Fraction (PF) 3 selected. Amino acids selected throughout an AccQ-Tag system. As a result, 17 species of amino acids and several species of unknown amino acids identified. Both fractions had the highest content of phenylalanine. This study identified the potential of biologically active and functional peptides derived from casein that affect the food and dairy industry.

• Food Science of Animal Resources
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• v.29 no.5
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• pp.633-639
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• 2009

The principal objective of the current study was to prepare low molecular weight peptides from milk proteins using enzymatic hydrolysis techniques, in an effort to assess the antioxidant activity of these peptides. The casein and whey proteins isolated from fresh milk were treated with several proteolytic enzymes, such as chymotrypsin, pepsin, and trypsin and the resulting low molecular weight peptides were collected by TCA precipitation. Their identity was confirmed by SDS-PAGE analysis. The hydrolysis experiments indicated that whey protein treated with chymotrypsin displayed the highest degree of protein hydrolysis. The antioxidant activity of milk protein hydrolysates was determined by measuring the ABTS-radical scavenging activity. The results of these experiments showed that hydrolysis of the milk protein was effective in increasing their antioxidant activities. Especially, the tryptic digested casein displayed the highest radical scavenging activity (80.7%). The hydrolyzed low molecular weight milk protein was isolated using an ultrafiltration membrane. The casein hydrolysate passed through a membrane with molecular weight cut-off (MWCO) of 3 kDa displayed the strongest antioxidant activity.

• Applied Biological Chemistry
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• v.34 no.4
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• pp.327-333
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• 1991

This study was carried out to determine the effects of media compositions on cell growth and casein hydrolysis for cell production in order to add Micrococcus sp. LL3 as a potential agent for industrial application for the shortening of ripening period. Monosaccharides like glucose, mannose and fructose were mare excellent as carbon source, but arabinose and xylose markedly inhibited cell growth and caseinolysis. Among the organic nutrients, yeast extract was more effective for cell growth and for caseolysis. However, inorganic nitrogen sources were less effective than organic sources. Urea inhibited cell growth severely. Cell growth and caseinolysis were rather increased a little in the broth containing 1% NaCl, and the organism tolerated and grew in relatively high concentrations of NaCl up to 9%. Addition of vitamin did not affect cell growth and caseolysis in level of $0.1\;{\mu}g/ml$ concentration. Cell growth and caseinolysis were stimulated by addition of glutamic acid and $MgSO_4$ with concentration of 0.2% and 0.05% respectively.

• Journal of Life Science
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• v.20 no.11
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• pp.1656-1661
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• 2010

Alkaline protease for the hydrolysis of egg yolk protein was immobilized on five carriers - Duolite A568, Celite R640, Dowex-1, Dowex 50W and Silica gel R60. Duolite A568 showed a maximum immobilization yield of 24.7%. Optimum pH for the free and immobilized enzyme was pH 8 and 9, respectively. However, no change was observed in optimum temperature ($50^{\circ}C$). Thermal stability was observed in immobilized enzymes compared to free enzymes. The immobilized enzyme retained 86% activity after 10 cycle operations in a repeated batch process. The effect of flow rate on the stability of enzyme activity in continuous packed-bed reactor was investigated. Lowering flow rate increased the stability of the immobilized enzyme. After 96 hr of continuous operation in a packed-bed reactor, the immobilized enzyme retained 83 and 61% activity when casein and egg yolk were used as a raw materials, respectively.

• Food Science and Preservation
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• v.13 no.1
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• pp.88-94
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• 2006

This study was carried out to produce antimicrobial peptides from casein using various proteases. To examine whether the hydrolysis of casein would produce antimicrobial substance and the application as natural antimicrobial material, casein was hydrolyzed by five different proteases. The casein hydrolysate was fractionated with regenerated membrane filter (molecular weight cut-off 30,000 10,000 and 3,000) and antimicrobial activity was measured for each fraction. Antimicrobial activity appeared great in the fraction below 3,000 molecular weight The fraction was re-fractionated by high performance liquid chromatography and substance of main peak (retention time: 13.2 min) collected was used as a sample to measure antimicrobial activity. Among the casein hydrolysates produced by protease, antimicrobial activity was observed the greatest in hydrolysate treated with Aspergillus oryzae protease. The minimum inhibition concentrations of the Asp. oryzae protease hydrolysate were 1.0-1.5 mg/mL. This hydrolysate was a heat stable peptide since antimicrobial activity was maintained after treating with heat for 20 min at $121^{\circ}C$.

• Korean Journal of Food Science and Technology
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• v.27 no.5
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• pp.794-798
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• 1995

Deamidation by neutrase on glutaminyl and asparaginyl residues of protein was examined. The optimum pH and temperature for BSA(bovine serum albumin) deamidation by neutrase were 10 and $20^{\circ}C$, respectively. The incubation for 3 hrs under the optimum condition removed 24% of amide groups and hydrolyzed 2.9% of peptide bonds. Deamidation by neutrase was superior to that by pronase, bromelain, or ficin. Deamidation degrees of egg albumin, soy protein isolate and casein by neutrase under the optimum condition were about 20%, 14% and 14%, respectively. However, relatively high degree of peptide hydrolysis was accompanied with casein deamidation.

• Journal of the Korean Society of Food Science and Nutrition
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• v.31 no.2
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• pp.263-270
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• 2002

In the recent studies, many researchers are interested in foods as functional components rather than nutrient sources. Cow's milk is considered as an excellent food sources because of its many nutrients. Casein is a major milk protein and has been reported to have hyperlipidemic and hypercholesterolemic effects. But several reporters have suggested that peptide fractions and hydrolysate of casein have hypolipidemic effects differing from intact protein, casein. Therefore, the objective of the study was to investigate how the casein peptide fractions affect lipid metabolism in rats fed normal or high fat diets. The peptide fractions and hydrolysate of casein were obtained by casein hydrolysis with trypsin. The male rats (Sprague-Dawley), weighing approximately 150 g, were fed each experimental diet containing casein (CAS), casein hydrolysate (CH), casein hydrolysate precipitate (Cpt) and two kinds of peptide fractions (CL & CB) for three weeks, respectively. In the exit I, the male rats were fed normal fat diets (7% soybean oil & cholesterol-free; Expt. I), and in the expt II, fed high fat diets (18% beef tallow & 1% cholesterol; Expt. II). Crude protein contents were calculated from nitrogen contents. Amino acid composition of each fraction was also analyzed. The concentration of total lipid, total cholesterol and triglyceride in serum, liver and feces were measured. As the results of study, tole rats fed peptide fractions with normal fat diets (Expt. I) had no effects on total lipid, total cholesterol and triglyceride concentration in serum and liver and fecal excretion. However, in the rats fed hydrophobic casein peptide fractions (CB) with high fat diet, fecal lipids excretion were significantly increased and the lipids concentration of serum and those of liver tended to decrease, numerically.

• Food Science of Animal Resources
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• v.29 no.6
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• pp.659-667
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• 2009

Casein is considered to be the main source of protein in milk; therefore, many studies have been conducted to identify casein-derived bioactive peptides and their physiological effects. Casein is inactive within the parent protein but can be liberated by various proteases and enzymatic hydrolysis during microbial fermentation and gastrointestinal digestion. Once absorbed, casein exhibits different bioavailabilities in the body. Specifically, casein-derived peptides function as angiotensin converting enzyme (ACE) inhibitor in the cardiovascular system; thus, they are expected to reduce and prevent hypertension. Additionally, casein-derived peptides behave as opioid-like peptides in the nervous system, which impacts relaxation. These peptides are also expected to modulate various aspects of immune functions. Finally, caseinophosphopeptide (CPP) and glycomacropeptide (GMP) may exhibit a number of nutritional effects such as the absorption of calcium, iron or zinc. Many studies have been conducted to evaluate casein-derived peptides due to their multifunctional properties and the results of these studies have contributed to the development of a wide variety of functional dairy products. The purpose of this paper was to review the generation of bioactive peptides, their absorption and metabolism, and their specific bioactive effects.