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...
Main Authors: | , , , , , |
---|---|
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/ |
id |
doaj-e6f97b3bb04748fd862ca172f17d2ac5 |
---|---|
record_format |
Article |
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 |
_version_ |
1725592732095741952 |