Antioxidant Activities of Hydrolysates of Arca Subcrenata Prepared with Three Proteases

In order to get products with antioxidant activity from Arca subcrenata Lischke, the optimal hydrolase and hydrolysis conditionswere investigated in the paper. Three proteases (neutrase, alcalase and papain) were applied to hydrolyze the homogenate of A. subcrenata. An orthogonaldesign was used to o...

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Main Authors: Liyan Song, Tingfei Li, Rongmin Yu, Chunyan Yan, Yu Zhao, Shengfang Ren
Format: Article
Language:English
Published: MDPI AG 2008-11-01
Series:Marine Drugs
Subjects:
Online Access:http://www.mdpi.com/1660-3397/6/4/607/
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spelling doaj-e6f97b3bb04748fd862ca172f17d2ac52020-11-24T23:14:57ZengMDPI AGMarine Drugs1660-33972008-11-016460761910.3390/md6040607Antioxidant Activities of Hydrolysates of Arca Subcrenata Prepared with Three ProteasesLiyan SongTingfei LiRongmin YuChunyan YanYu ZhaoShengfang RenIn order to get products with antioxidant activity from Arca subcrenata Lischke, the optimal hydrolase and hydrolysis conditionswere investigated in the paper. Three proteases (neutrase, alcalase and papain) were applied to hydrolyze the homogenate of A. subcrenata. An orthogonaldesign was used to optimize hydrolysis conditions, and the pH-stat methods was used to determine the degree of hydrolysis. Viewed from the angle ofreducing power, such as scavenging activities against α,α-diphenyl-β-picrylhydrazyl (DPPH) radical and hydrogen peroxide, the antioxidantactivities of the alcalase hydrolysate (AH) were superior to neutrase hydrolysate (NH) and papain hydrolysate (PH), and its EC50 values in DPPHradical and hydrogen peroxide scavenging effect were 6.23 mg/ml and 19.09 mg/ml, respectively. Moreover, compared with products hydrolyzed byneutrase and papain, the molecular mass of AH was lower and its content ofamino acid of peptides was higher. Therefore, alcalase was selected as theoptimal enzyme to produce active ingredients since its hydrolysate exhibitedthe best antioxidant activity among them and possessed large amount ofpotential active peptides.http://www.mdpi.com/1660-3397/6/4/607/Arca subcrenata Lischkehydrolysatesantioxidant activityprotease
collection DOAJ
language English
format Article
sources DOAJ
author Liyan Song
Tingfei Li
Rongmin Yu
Chunyan Yan
Yu Zhao
Shengfang Ren
spellingShingle Liyan Song
Tingfei Li
Rongmin Yu
Chunyan Yan
Yu Zhao
Shengfang Ren
Antioxidant Activities of Hydrolysates of Arca Subcrenata Prepared with Three Proteases
Marine Drugs
Arca subcrenata Lischke
hydrolysates
antioxidant activity
protease
author_facet Liyan Song
Tingfei Li
Rongmin Yu
Chunyan Yan
Yu Zhao
Shengfang Ren
author_sort Liyan Song
title Antioxidant Activities of Hydrolysates of Arca Subcrenata Prepared with Three Proteases
title_short Antioxidant Activities of Hydrolysates of Arca Subcrenata Prepared with Three Proteases
title_full Antioxidant Activities of Hydrolysates of Arca Subcrenata Prepared with Three Proteases
title_fullStr Antioxidant Activities of Hydrolysates of Arca Subcrenata Prepared with Three Proteases
title_full_unstemmed Antioxidant Activities of Hydrolysates of Arca Subcrenata Prepared with Three Proteases
title_sort antioxidant activities of hydrolysates of arca subcrenata prepared with three proteases
publisher MDPI AG
series Marine Drugs
issn 1660-3397
publishDate 2008-11-01
description In order to get products with antioxidant activity from Arca subcrenata Lischke, the optimal hydrolase and hydrolysis conditionswere investigated in the paper. Three proteases (neutrase, alcalase and papain) were applied to hydrolyze the homogenate of A. subcrenata. An orthogonaldesign was used to optimize hydrolysis conditions, and the pH-stat methods was used to determine the degree of hydrolysis. Viewed from the angle ofreducing power, such as scavenging activities against α,α-diphenyl-β-picrylhydrazyl (DPPH) radical and hydrogen peroxide, the antioxidantactivities of the alcalase hydrolysate (AH) were superior to neutrase hydrolysate (NH) and papain hydrolysate (PH), and its EC50 values in DPPHradical and hydrogen peroxide scavenging effect were 6.23 mg/ml and 19.09 mg/ml, respectively. Moreover, compared with products hydrolyzed byneutrase and papain, the molecular mass of AH was lower and its content ofamino acid of peptides was higher. Therefore, alcalase was selected as theoptimal enzyme to produce active ingredients since its hydrolysate exhibitedthe best antioxidant activity among them and possessed large amount ofpotential active peptides.
topic Arca subcrenata Lischke
hydrolysates
antioxidant activity
protease
url http://www.mdpi.com/1660-3397/6/4/607/
work_keys_str_mv AT liyansong antioxidantactivitiesofhydrolysatesofarcasubcrenatapreparedwiththreeproteases
AT tingfeili antioxidantactivitiesofhydrolysatesofarcasubcrenatapreparedwiththreeproteases
AT rongminyu antioxidantactivitiesofhydrolysatesofarcasubcrenatapreparedwiththreeproteases
AT chunyanyan antioxidantactivitiesofhydrolysatesofarcasubcrenatapreparedwiththreeproteases
AT yuzhao antioxidantactivitiesofhydrolysatesofarcasubcrenatapreparedwiththreeproteases
AT shengfangren antioxidantactivitiesofhydrolysatesofarcasubcrenatapreparedwiththreeproteases
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