Effect of bambara groundnut protein isolate on autolysis and gel properties of surimi from threadfin bream (Nemipterus bleekeri)

被引：103

作者：

Oujifard, Amin ^{[2
]}

Benjakul, Soottawat ^{[1
]}

Ahmad, Mehraj ^{[1
]}

Seyfabadi, Jafar ^{[3
]}

机构：

[1] Prince Songkla Univ, Fac Agroind, Dept Food Technol, Hat Yai 90112, Songkhla, Thailand

[2] Persian Gulf Univ, Fac Agr & Nat Resources, Dept Fisheries, Borazjan, Bushehr, Iran

[3] Tarbiat Modares Univ, Fac Marine Sci, Dept Marine Biol, Noor, Mazandaran, Iran

来源：

LWT-FOOD SCIENCE AND TECHNOLOGY | 2012年 / 47卷 / 02期

关键词：

Autolytic activity; Bambara groundnut; Surimi; Threadfin bream; Gel; Inhibitor; BOUND SERINE PROTEINASE; PACIFIC WHITING SURIMI; PRIACANTHUS-TAYENUS; PLASMA-PROTEIN; BIGEYE SNAPPER; INHIBITORS; MODORI; FISH; PURIFICATION; DEGRADATION;

D O I：

10.1016/j.lwt.2012.01.016

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

Impact of bambara groundnut protein isolate (BGPI) on autolysis and gel properties of surimi from threadfin bream (Nemipterus bleekeri) was investigated. BGPI with trypsin inhibitory activity of 6356.3 +/- 6.02 unit/g markedly increased (P < 0.05) the breaking force and deformation of modori gel as the levels used (0-3 g/100 g) increased. Nevertheless, only 0.25 g/100 g BGPI increased breaking force and deformation of kamaboko gel and increasing BGPI levels showed detrimental effect on gelation. Myosin heavy chain (MHC) was more retained when BGPI concentration increased, especially in modori gel. However, whiteness slightly decreased (P < 0.05) with increasing BGPI levels. Microstructure of kamaboko gel added with 0.25 g/100 g BGPI had finer and more ordered fibrillar structure than that without BGPI addition. Therefore, BGPI at an appropriate level could be an alternative food-grade inhibitor to improve gel properties of surimi. (C) 2012 Elsevier Ltd. All rights reserved.

引用

页码：261 / 266

页数：6

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