Thermal stability of fish natural actomyosin affects reactivity to cross-linking by microbial and fish transglutaminases

被引：38

作者：

Hemung, Bung-Orn ^{[1
]}

Li-Chan, Eunice C. Y. ^{[2
]}

Yongsawatdigul, Jirawat ^{[1
]}

机构：

[1] Suranaree Univ Technol, Inst Agr Technol, Sch Food Technol, Nakhon Ratchasima 30000, Thailand

[2] Univ British Columbia, Fac Land & Food Syst, Food Nutr & Hlth Program, Vancouver, BC V5Z 1M9, Canada

来源：

FOOD CHEMISTRY | 2008年 / 111卷 / 02期

关键词：

threadfin bream; pacific whiting; transglutaminase; natural actomyosin; thermal stability;

D O I：

10.1016/j.foodchem.2008.04.014

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

Natural actomyosin (NAM) from Pacific whiting (PW) showed thermal transition temperatures by circular dichroism at 31.8 and 43.1 degrees C, which were lower than those of threadfin bream (TB) NAM, 35.0 and 49.3 degrees C. Enclothermic transitions of PW-NAM by differential scanning calorimetry were at 31.8, 42.1 and 75.3 degrees C, compared to 36.1, 50.9 and 78.4 degrees C for TB-NAM. Based on surface hydrophobicity, a-helical content, and solubility, PW-NAM unfolded to a greater extent than did TB-NAM when incubated at 25 degrees C for 4 h and 40 degrees C for 2 h, suggesting its lower thermal stability. Transglutaminase generally catalyzed more extensive cross-linking of PW-myosin heavy chain (MHC) than TB-MHC, and the MHC cross-linking mediated by microbial transglutaminase (MTG) was greater than by fish transglutaminase (FTG). Textural properties of PW-NAM gels increased approximately 3.6-6.1-fold and 1.3-1.5-fold in the presence of MTG and FTG, respectively. (C) 2008 Elsevier Ltd. All rights reserved.

引用

页码：439 / 446

页数：8

共 33 条

[1] Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes [J].