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ANTIOXIDANT AND ACE INHIBITORY PROPERTIES OF POULTRY VISCERA PROTEIN HYDROLYSATE AND ITS PEPTIDE FRACTIONS
Author(s) -
JAMDAR S.N.,
RAJALAKSHMI V.,
SHARMA ARUN
Publication year - 2012
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.2011.00562.x
Subject(s) - hydrolysate , antioxidant , chemistry , peptide , ultrafiltration (renal) , ic50 , food science , angiotensin converting enzyme , biochemistry , fractionation , chromatography , in vitro , hydrolysis , biology , endocrinology , blood pressure
Poultry viscera protein hydrolysate (PVPH) was fractionated using ultrafiltration membrane into three peptide fractions viz. Fractions I (>10 kDa), II (3–10 kDa) and III (<3 kDa) with yield of 13.4, 18.4 and 66.6%, respectively. Antioxidant activity of PVPH and its fractions was determined in terms of radical‐scavenging activity (RSA), reducing power (RP), total antioxidant activity (TAA) and antioxidant activity index (AAI). PVPH exhibited excellent RSA and TAA at peptide concentration of 0.2 and 2.0 mg/mL, respectively. It also showed RP value as 0.4, and AAI as 500 after 100 min at peptide concentration of 9 and 30 mg/mL, respectively. Scavenging of 2, 2′‐azinobis (3‐ethyl‐benzothiazoline‐6 sulfonic acid) and hydroxyl radicals by Fraction III was found to be significantly higher than other fractions, while superoxide scavenging activity was independent of peptide size. Fraction I exhibited better RP, TAA and AAI. PVPH and Fraction III showed the highest angiotensin‐converting enzyme (ACE) inhibitory activity (IC 50 = 0.34 mg/mL). PRACTICAL APPLICATIONS Poultry viscera are an underutilized by‐product of poultry processing industry. A rapid autolytic method was developed in our laboratory to prepare a hydrolysate from this tissue. In order to find the potential application of this value‐added product, antioxidant and angiotensin‐converting enzyme inhibitory properties of the peptide fractions of the hydrolysate were evaluated.