Effects of fish protein hydrolysate and freeze-thaw treatment on physicochemical and gel properties of natural actomyosin from Pacific cod

被引：57

作者：

Korzeniowska, Malgorzata ^{[1
,2
]}

Cheung, Imelda W. Y. ^{[1
]}

Li-Chan, Eunice C. Y. ^{[1
]}

机构：

[1] Univ British Columbia, Fac Land & Food Syst, Food Nutr & Hlth Program, Vancouver, BC V6T 1Z4, Canada

[2] Wroclaw Univ Environm & Life Sci, Fac Food Sci, Dept Anim Prod Technol & Qual Management, PL-50375 Wroclaw, Poland

来源：

FOOD CHEMISTRY | 2013年 / 138卷 / 2-3期

基金：

加拿大自然科学与工程研究理事会;

关键词：

Cryoprotection; Fish protein hydrolysate; Surface hydrophobicity; Natural actomyosin; Texture analysis; Differential scanning calorimetry; STRUCTURAL-CHANGES; THERMAL-STABILITY; FROZEN STORAGE; MUSCLE; SURIMI; DENATURATION; MYOSIN;

D O I：

10.1016/j.foodchem.2012.09.150

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

The properties of natural actomyosin (NAM) containing 2% or 8% fish protein hydrolysate (FPH-2, FPH-8) or 8% sucrose-sorbitol blend (SuSo) were compared to control NAM before and after freeze-thaw treatment. Surface hydrophobicity of control and FPH-2 increased after freeze-thaw treatment, while that of FPH-8 did not change, which may be related to greater thermostability of actin and myosin in FPH-8 as observed by differential scanning calorimetry. The cooked gel of freeze-thawed control had 39% expressible moisture after an 8.5% cook loss, whereas gels of freeze-thawed SuSo, FPH-2 and FPH-8 had significantly lower expressible moisture (15-22%) and no cook loss. Gels of freeze-thawed FPH-2 and FPH-8 were similar to unfrozen control gel in hardness, cohesiveness and gumminess. This study demonstrates that FPH effectively stabilised NAM protein structure and function during freeze-thaw treatment. (C) 2012 Elsevier Ltd. All rights reserved.

引用

页码：1967 / 1975

页数：9

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