scholarly journals Purification and identification of five novel antioxidant peptides from goat milk casein hydrolysates

2013 ◽  
Vol 96 (7) ◽  
pp. 4242-4251 ◽  
Author(s):  
Z. Li ◽  
A. Jiang ◽  
T. Yue ◽  
J. Wang ◽  
Y. Wang ◽  
...  
Keyword(s):  
Goat Milk ◽  
Antioxidant Peptides ◽  
Milk Casein ◽  
Casein Hydrolysates

scholarly journals Effect of Temperature, pH, Enzyme to Substrate Ratio, Substrate Concentration and Time on the Antioxidative Activity of Hydrolysates from Goat Milk Casein by Alcalase

2016 ◽  
Vol 20 (2) ◽  
pp. 29-38 ◽  
Author(s):  
Guowei Shu ◽  
Bowen Zhang ◽  
Qian Zhang ◽  
Hongchang Wan ◽  
Hong Li
Keyword(s):  
Substrate Concentration ◽  
Superoxide Radical ◽  
Radical Scavenging Activity ◽  
Radical Scavenging ◽  
Goat Milk ◽  
Scavenging Activity ◽  
Antioxidant Peptides ◽  
Hydrolysis Time ◽  
Hydrolysis Temperature ◽  
Milk Casein

Abstract The effect of hydrolysis temperature (45, 50, 55, 60 and 65°C), pH (7.0, 7.5, 8.0, 8.5 and 9.0), enzyme to substrate (E/S) ratio (1.0, 1.5, 2.0, 2.5 and 3.0%), substrate concentration (2, 3, 4, 5 and 6%) and hydrolysis time (30-240min) on antioxidant peptides hydrolysated from goat’s milk casein by Alcalase was investigated using single factor experiment. In order to obtain high DPPH radical-scavenging activity, metal-chelating activity and superoxide radical scavenging activity, the optimal conditions were hydrolysis time of 150 min, temperature of 50°C, pH 8.0, E/S ratio of 2.0% and substrate concentration of 4.0%. The hydrolysis time, hydrolysis temperature, pH, E/S ratio and substrate concentration had a significant influence on degree of hydrolysis, metal-chelating activity, DPPH and superoxide radical scavenging activity on casein hydrolysate of goat milk by Alcalase, the results were beneficial for further provide theoretical basis for production of antioxidant peptides.

scholarly journals Enzymolysis Technology Optimization for Production of Antioxidant Peptides from Goat Milk Casein

2017 ◽  
Vol 21 (1) ◽  
pp. 51-60 ◽  
Author(s):  
Guowei Shu ◽  
Zhuo Wang ◽  
Li Chen ◽  
Qian Zhang ◽  
Ni Xin
Keyword(s):  
Free Radicals ◽  
Radical Scavenging Activity ◽  
Radical Scavenging ◽  
Casein Hydrolysate ◽  
Goat Milk ◽  
Process Conditions ◽  
Scavenging Activity ◽  
Antioxidant Peptides ◽  
Hydrolysis Time ◽  
Milk Casein

AbstractAntioxidant peptides can inhibit lipid peroxidation and scavenging free radicals, maintain the balance of free radicals, and against a variety of diseases. Response surface methodology was used to optimize process conditions for producing antioxidative peptides from goat’s milk casein hydrolysate with Alcalase. The results suggested that the optimal process parameters were: temperature at 62.5°C, pH 8.9, E/S ration at 2.5%, substrate concentration at 4.4% and hydrolysis time was 173min). Metal-chelating effect, superoxide anion radical scavenging activity and 1, 1-diphenyl-2-picrylhydrazyl (DPPH) free radical scavenging activity were shown to be 87.21±0.88%, 49.18±1.42% and 69.07±1.26% respectively under the optimal condition. The actual and predicated value were closely which indicated the optimized data fit well to model and the optimized parameters are reliable.

scholarly journals In Vitro Assessment of Antioxidative Potential of Goat Milk, Casein and its Hydrolysates: Comparison of Goat Milk with Bovine and Buffalo milk

2021 ◽  
Author(s):  
Sunny Kalyan ◽  
SUNITA MEENA ◽  
Suman Kapila ◽  
Radha Yadav ◽  
Gaurav Kr Deshwal
Keyword(s):  
Goat Milk ◽  
Raw Milk ◽  
Buffalo Milk ◽  
Cow Milk ◽  
Effect Of Temperature ◽  
In Vitro Assessment ◽  
Gastrointestinal Enzymes ◽  
Milk Casein ◽  
Casein Hydrolysates

Abstract The present study was executed with an aim to explore the antioxidative potential of goat, cow, and buffalo milk. Buffalo milk has showed highest antioxidative potential than goat and cow milk as measured by ABTS, ORAC, and DPPH assays, whereas goat milk has showed better antioxidative potential than cow milk when measured by ORAC and DPPH. Further, the effect of temperature on the antioxidative potential of goat milk was assessed. An increase in temperature has a negatively affect the antioxidative potential of goat milk. The antioxidative potential of goat milk was in the following order: raw milk > pasteurized milk > boiled milk. Casein derived from goat milk by isoelectric precipitation was hydrolyzed by gastrointestinal enzymes pepsin (P), trypsin (T), chymotrypsin (C), and their combinations PT, PC, TC, and PTC. Among all the casein hydrolysates, the maximum antioxidative potential was found in PT hydrolysate, further fractionated by 10, 3 and 1 kDa ultrafiltration membranes. 3–10 kDa fraction exhibited maximum antioxidative potential in comparison to other fractions of PT hydrolysate. Our results suggested that antioxidative potential of goat milk and its hydrolysates could be an important mean to obtain natural antioxidative peptides.

scholarly journals pH-shifting formation of goat milk casein nanoparticles from insoluble peptide aggregates and encapsulation of curcumin for enhanced dispersibility and bioactivity

LWT ◽  
2021 ◽  
pp. 112753
Author(s):  
Xiaojing Du ◽  
Huijuan Jing ◽  
Li Wang ◽  
Xin Huang ◽  
Ling Mo ◽  
...  
Keyword(s):  
Goat Milk ◽  
Ph Shifting ◽  
Milk Casein

Fractionation and identification of novel antioxidant peptides from buffalo and bovine casein hydrolysates

2017 ◽  
Vol 232 ◽  
pp. 753-762 ◽  
Author(s):  
Ahmed Behdal Shazly ◽  
Zhiyong He ◽  
Mahmoud Abd El-Aziz ◽  
Maomao Zeng ◽  
Shuang Zhang ◽  
...  
Keyword(s):  
Antioxidant Peptides ◽  
Casein Hydrolysates

scholarly journals Protein-polyphenol reactions

1982 ◽  
Vol 47 (2) ◽  
pp. 191-211 ◽  
Author(s):  
R. F. Hurrell ◽  
P. A. Finot ◽  
J. L. Cuq
Keyword(s):  
Caffeic Acid ◽  
Goat Milk ◽  
Lysine Content ◽  
Reaction Products ◽  
Protein Ratio ◽  
Alkaline Conditions ◽  
Available Lysine ◽  
Sunflower Protein ◽  
Milk Casein ◽  
Net Protein

1. Studies were made on the lysine content of casein reacted with caffeic acid oxidized aerobically under alkaline conditions or enzymically with tyrosinase (EC 1.14.18.1).2. Loss of fluorodinitrobenzene (FDNB)-reactive lysine was rapid at pH 10 and increased with time and the temperature of the reaction, with concentration of caffeic acid and with the oxygenation of the mixture. In presence of the enzyme mushroom tyrosinase, maximum reduction of reactive lysine occurred at pH 7 and was dependent on the reaction time and on the concentration of caffeic acid.3. Reaction of α-formyl-L-[U- 14C]lysine with caffeic acid at pH 10 showed the rapid formation of five reaction products which appeared to polymerize gradually as the reaction progressed.4. The nutritionally available lysine content of the casein-caffeic acid mixtures, as assayed with rats, was reduced after both alkaline and enzymic reactions, as were faecal digestibility, net protein ratio and net protein utilization. Biological value however was not reduced.5. In metabolic studies using goat milk casein labelled with L-[3H]lysine and reacted with caffeic acid in the same way, the lysine–caffeoquinone reaction products were not absorbed by the rat but were excreted directly in the faeces.6. The importance of the reaction of proteins with caffeoquinone and chlorogenoquinone (formed by the oxidation of caffeic and chlorogenic acids respectively) is discussed in relation to the production of sunflower protein, leaf protein and other vegetable-protein concentrates.

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