The effects of sodium bicarbonate on conformational changes of natural actomyosin from Pacific white shrimp (Litopenaeus vannamei)

被引：49

作者：

Chantarasuwan, Chakkawat ^{[1
]}

Benjakul, Soottawat ^{[1
]}

Visessanguan, Wonnop ^{[2
]}

机构：

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

[2] Natl Sci & Technol Dev Agcy, Natl Ctr Genet Engn & Biotechnol, Klongluang 12120, Pathumthani, Thailand

来源：

FOOD CHEMISTRY | 2011年 / 129卷 / 04期

关键词：

Physicochemical changes; Natural actomyosin; Sodium bicarbonate; Pacific white shrimp; Muscle protein; DENATURATION MECHANISM; PRESSURE TREATMENT; STRUCTURAL-CHANGES; SULFHYDRYL-GROUPS; MUSCLE PROTEINS; INJECTION; STORAGE; SURIMI; MYOSIN; ACTIN;

D O I：

10.1016/j.foodchem.2011.06.023

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

Changes in natural actomyosin (NAM) from Pacific white shrimp (Litopenaeus vannamei) treated with sodium bicarbonate (NaHCO(3)) at different concentrations (0-1 M) in the absence or the presence of 2.5% NaCl were studied. Turbidity of NAM solutions decreased with coincidental increase in solubility as the concentration of NaHCO(3) increased. Surface hydrophobicity (S(o)ANS) and total sulfhydryl content of NAM also increased when NaHCO(3) concentration increased. Greater decreases in Ca(2+)- and Mg(2+)-ATPase activity were found in all NAM as NaHCO(3) concentration increased, suggesting the denaturation of myosin head and the dissociation of actomyosin complex. The zeta potential (zeta) analysis suggested that the surface of NAM became more negatively charged (-12.12 to -26.98) as NaHCO(3) concentration increased. Those changes were more intense in the presence of 2.5% NaCl. Transmission electron microscopy showed that the structure of actomyosin was more dissociated and lost the filamental structure when NaHCO(3) at higher levels was used. (C) 2011 Elsevier Ltd. All rights reserved.

引用

页码：1636 / 1643

页数：8

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