Impact of sequential enzymatic hydrolysis on antioxidant activity and peptide profile of casein hydrolysate
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ORIGINAL ARTICLE
Impact of sequential enzymatic hydrolysis on antioxidant activity and peptide profile of casein hydrolysate Priyanka Singh Rao1
•
Rajesh Bajaj1 • Bimlesh Mann1
Revised: 6 December 2019 / Accepted: 29 April 2020 Ó Association of Food Scientists & Technologists (India) 2020
Abstract This paper shows the potential of dual enzyme approach on antioxidant activity of casein hydrolysates. Casein was hydrolysed using the proteolytic enzymes alcalase, flavourzyme in isolation and in sequential order. Casein hydrolysates were evaluated for the degree of hydrolysis, antioxidant activity, molecular weight distribution patterns and peptide sequence. Casein hydrolysate produced by the sequential hydrolysis of alcalase and flavourzyme showed higher degree of hydrolysis and antioxidant activity as compared to hydrolysate obtained by individual enzymes. In size exclusion chromatograph of casein hydrolysate S3, peptides with molecular weight of
0.57 kDa share 12% area in total area of chromatogram which was 10 times higher than that of hydrolysate S1 and nearly half of that of hydrolysate S2. On subjecting to HPLC-TOF-ESI separation potential antioxidant peptides were identified. The peptide sequence VLPVPQ along with potential fragments was identified in hydrolysate S1 and S2 and HPHPHLS along with its potential sequence was identified in hydrolysate S1, S2 and S3. Sequential hydrolysis of casein showed better antioxidant activity and peptide profile in less duration as compared to the casein hydrolysate obtained by individual enzyme.
Electronic supplementary material The online version of this article (https://doi.org/10.1007/s13197-020-04495-2) contains supplementary material, which is available to authorized users. & Priyanka Singh Rao [email protected] & Rajesh Bajaj [email protected] Bimlesh Mann [email protected] 1
Dairy Chemistry Division, National Dairy Research Institute, Karnal, Haryana 132001, India
123
J Food Sci Technol
Graphic abstract
Keywords Casein Enzymatic hydrolysis Alcalase Flavourzyme Antioxidant activity Peptide profile
Introduction Antioxidants are molecules that protect biological systems either by inhibiting or preventing the oxidation of substrate by free radicals (Serafini 2006). Proteins have excellent potential as antioxidant additives in foods because they can inhibit lipid oxidation through multiple pathways including inactivation of reactive oxygen species, scavenging free radicals, chelation of pro-oxidative transition metals, reduction of hydro peroxides and alteration of the physical properties of food systems. Recently, there has been a particular focus on foodderived peptides as a source of antioxidants. Antioxidant activity of the peptides is due to the characteristic amino acid sequence of derived peptides, depending upon the protease activity. Antioxidative peptides are usually composed of 5–11 amino acids; the most reactive are either sulfur-containing side chains (cysteine and methionine) or aromatic side chains (tryptophan, tyrosine,
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