2011Journal of Guangxi UniversityRequires access

Optimization of enzymatic hydrolysis conditions parameters for antioxidant capacity of hydrolysates from protein of Tilapia heels

Dankui Liao

Open publisher page 2 citations

Abstract

Antioxidant peptide can inhibit radical scavenging activities and be obtained by hydrolysis some proteins.The tilapia heels protein was hydrolyzed with four kinds of enzymes.Antioxdant activity was investigated using radical scavenging activity assay for superoxide free radical(O2-·),1,1-diphenyl-2-picrylhydrazine(DPPH·) and linoleic acid peroxidation for the hydrolysates from different hydrolysis times with four kinds of enzymes.The results showed that the hydrlysate with alikaline protease had a high antioxidant activity.The optimal hydrolysis conditions obtained from experiment was the enzyme concentration of 2000U/g,substrate concentration of 3%,temperature of 50 ℃,pH of 9.5 and hydrolysis time of 4 h.Meanwhile,the degree of hydrolysis was 24.21%,and the radical scavenging efficient was 36.24% for O2-·,76.91% for DPPH· and 66.87% for linoleic acid peroxidation,respectively.Therefore,preparation of antioxidant polypeptide by hydrolysis of the tilapia heels protein was feasible.

About this research paper

What this paper is about

Antioxidant peptide can inhibit radical scavenging activities and be obtained by hydrolysis some proteins.The tilapia heels protein was hydrolyzed with four kinds of enzymes.Antioxdant activity was investigated using radical scavenging activity assay for superoxide free radical(O2-·),1,1-diphenyl-2-picrylhydrazine(DPPH·) and linoleic acid peroxidation for the hydrolysates from different hydrolysis times with four kinds of enzymes.The results showed that the hydrlysate with alikaline protease had a high antioxidant activity.The optimal hydrolysis conditions obtained from experiment was the enzyme concentration of 2000U/g,substrate concentration of 3%,temperature of 50 ℃,pH of 9.5 and hydrolysis time of 4 h.Meanwhile,the degree of hydrolysis was 24.21%,and the radical scavenging efficient was 36.24% for O2-·,76.91% for DPPH· and 66.87% for linoleic acid peroxidation,respectively.Therefore,preparation of antioxidant polypeptide by hydrolysis of the tilapia heels protein was feasible.

Why it matters

OpenAlex reports 2 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

Antioxidant peptide can inhibit radical scavenging activities and be obtained by hydrolysis some proteins.The tilapia heels protein was hydrolyzed with four kinds of enzymes.Antioxdant activity was investigated using radical scavenging activity assay for superoxide free radical(O2-·),1,1-diphenyl-2-picrylhydrazine(DPPH·) and linoleic acid peroxidation for the hydrolysates from different hydrolysis times with four kinds of enzymes.The results showed that the hydrlysate with alikaline protease had a high antioxidant activity.The optimal hydrolysis conditions obtained from experiment was the enzyme concentration of 2000U/g,substrate concentration of 3%,temperature of 50 ℃,pH of 9.5 and hydrolysis time of 4 h.Meanwhile,the degree of hydrolysis was 24.21%,and the radical scavenging efficient was 36.24% for O2-·,76.91% for DPPH· and 66.87% for linoleic acid peroxidation,respectively.Therefore,preparation of antioxidant polypeptide by hydrolysis of the tilapia heels protein was feasible.

Key concepts: Chemistry, Hydrolysis, Antioxidant, DPPH, Hydrolysate, Enzymatic hydrolysis, Tilapia, Linoleic acid

Related papers

Back to paper searchBrowse research topicsOriginal source
Optimization of enzymatic hydrolysis conditions parameters for antioxidant capacity of hydrolysates from protein of Tilapia heels — Research Paper | ScholarLens