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

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.

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Protein-polyphenol reactions

British Journal Of Nutrition ◽

10.1079/bjn19820027 ◽

1982 ◽

Vol 47 (2) ◽

pp. 191-211 ◽

Cited By ~ 77

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

Journal of Dairy Science ◽

10.3168/jds.2012-6511 ◽

2013 ◽

Vol 96 (7) ◽

pp. 4242-4251 ◽

Cited By ~ 51

Author(s):

Z. Li ◽

A. Jiang ◽

T. Yue ◽

J. Wang ◽

Y. Wang ◽

...

Keyword(s):

Goat Milk ◽

Antioxidant Peptides ◽

Milk Casein ◽

Casein Hydrolysates

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

Acta Universitatis Cibiniensis Series E Food Technology ◽

10.1515/aucft-2017-0006 ◽

2017 ◽

Vol 21 (1) ◽

pp. 51-60 ◽

Cited By ~ 1

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.

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Identification of novel peptides from goat milk casein that ameliorate high-glucose-induced insulin resistance in HepG2 cells

Journal of Dairy Science ◽

10.3168/jds.2019-17513 ◽

2020 ◽

Vol 103 (6) ◽

pp. 4907-4918 ◽

Cited By ~ 3

Author(s):

H. Gong ◽

J. Gao ◽

Y. Wang ◽

Q.W. Luo ◽

K.R. Guo ◽

...

Keyword(s):

Insulin Resistance ◽

High Glucose ◽

Hepg2 Cells ◽

Goat Milk ◽

Milk Casein

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Rapid detection of cow milk adulteration/contamination in goat milk by a lateral flow colloidal gold immunoassay strip

Journal of Dairy Research ◽

10.1017/s0022029919000116 ◽

2019 ◽

Vol 86 (1) ◽

pp. 94-97 ◽

Cited By ~ 1

Author(s):

Bochao Liu ◽

Jinhong Si ◽

Fang Zhao ◽

Qi Wang ◽

Yu Wang ◽

...

Keyword(s):

Colloidal Gold ◽

Rapid Detection ◽

Goat Milk ◽

Lateral Flow ◽

Cow Milk ◽

Quantitative Detection ◽

Enzyme Linked Immunosorbent Assay ◽

Milk Adulteration ◽

Milk Casein ◽

Higher Sensitivity

AbstractCurrent available methods to detect cow milk adulteration or accidental contamination of goat milk are both laborious and time consuming. The aim of this technical research communication was to develop a simple, rapid, specific and sensitive method for quantitative detection of cow milk in goat milk. A competitive lateral flow immunoassay (LFIA) strip was developed using a specific monoclonal antibody (mAb) labeled with colloidal gold nanoparticles (GNPs) for specifically binding to cow milk casein. The detection limit of this rapid detection was 0.07% of cow milk in goat milk, providing equal specificity and higher sensitivity when compared with a commercial enzyme-linked immunosorbent assay (ELISA). These result suggest that the established rapid GNPs-LFIA strip could be used for monitoring cow milk adulteration/contamination of goat milk.

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