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Authors

FENG Rui, College of Food Science and Technology, Guangdong Ocean University, Zhanjiang, Guangdong 524088 ,China ;Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, Zhanjiang,Guangdong 524088 , China ;Guangdong Provincial Engineering Technology Research Center of Marine Food,Zhanjiang, Guangdong 524088 , China
HONG Peng-zhi, College of Food Science and Technology, Guangdong Ocean University, Zhanjiang, Guangdong 524088 ,China ;Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, Zhanjiang,Guangdong 524088 , China ;Guangdong Provincial Engineering Technology Research Center of Marine Food,Zhanjiang, Guangdong 524088 , China ;Southern Marine Science and Engineering Guangdong Laboratory〔Zhanjiang〕, Zhanjiang, Guangdong 524025 , China
YANG Ping, College of Food Science and Technology, Guangdong Ocean University, Zhanjiang, Guangdong 524088 ,China ;Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, Zhanjiang,Guangdong 524088 , China ;Guangdong Provincial Engineering Technology Research Center of Marine Food,Zhanjiang, Guangdong 524088 , China ;Southern Marine Science and Engineering Guangdong Laboratory〔Zhanjiang〕, Zhanjiang, Guangdong 524025 , China
ZHOU Chun-xia, College of Food Science and Technology, Guangdong Ocean University, Zhanjiang, Guangdong 524088 ,China ;Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, Zhanjiang,Guangdong 524088 , China ;Guangdong Provincial Engineering Technology Research Center of Marine Food,Zhanjiang, Guangdong 524088 , China ;Southern Marine Science and Engineering Guangdong Laboratory〔Zhanjiang〕, Zhanjiang, Guangdong 524025 , China

Abstract

Myosin was extracted from tilapia (Oreochromis niloti-cus) and the heat-induced gel was prepared, and the effect of CaCl2 addition on the water holding capacity, microstructure and chemical interactions of myosin gel was investigated under different salt conditions (1,50,150,600 mmol/L NaCl). The effects and mechanisms of Ca2+on thermal gel properties of myosin were determined under the low salt conditions. Experimental results showed that under the conditions of low salt concentration (1~150 mmol/L NaCl), there were weak opaque gels due to a rapid aggregation of myosin filaments during heating. These myosin gels exhibited a cross-linked network with coarse cross-linked strands and large cavities, and the water holding capacity of gels was low. Hydrophobic interactions were responsible for the heat-induced gel formation of myosin. During the gelation process, the addition of 10 mmol/L CaCl2 promoted the unfolding of myosin and caused α-helices to partially turn into β-sheets with the reduced hydrogen bond interactions, thus resulted in stronger disulfide linkages between myosin molecules (P<0.05), which contributed to the ordered and dense three-dimensional network with significantly improved water holding capacity of myosin gel (P<0.05). Moreover, this improvement was more obvious at 1 mmol/L NaCl. Therefore, an appropriate amount of CaCl2 can effectively improve the gel properties of myosin under low salt conditions.

Publication Date

5-28-2020

First Page

39

Last Page

45

DOI

10.13652/j.issn.1003-5788.2020.05.008

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