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The differences of muscle proteins between neon flying squid (Ommastrephes bartramii) and jumbo squid (Dosidicus gigas) mantles via physicochemical and proteomic analyses.
Shui, Shan-Shan; Yao, Hui; Jiang, Ze-Dong; Benjakul, Soottawat; Aubourg, Santiago P; Zhang, Bin.
Afiliação
  • Shui SS; Key Laboratory of Health Risk Factors for Seafood of Zhejiang Province, College of Food Science and Pharmacy, Zhejiang Ocean University, Zhoushan 316022, China.
  • Yao H; Key Laboratory of Health Risk Factors for Seafood of Zhejiang Province, College of Food Science and Pharmacy, Zhejiang Ocean University, Zhoushan 316022, China.
  • Jiang ZD; College of Food and Biological Engineering, Jimei University, Xiamen 361021, China.
  • Benjakul S; International Center of Excellence in Seafood Science and Innovation, Faculty of Agro-Industry, Prince of Songkla University, Songkhla 90112, Thailand.
  • Aubourg SP; Department of Food Technology, Marine Research Institute (CSIC), Vigo 36208, Spain.
  • Zhang B; Key Laboratory of Health Risk Factors for Seafood of Zhejiang Province, College of Food Science and Pharmacy, Zhejiang Ocean University, Zhoushan 316022, China. Electronic address: zhangbin@zjou.edu.cn.
Food Chem ; 364: 130374, 2021 Dec 01.
Article em En | MEDLINE | ID: mdl-34147869
ABSTRACT
Neon flying squid (OB) and jumbo squid (DG) mantles were evaluated to reveal the similarities and differences in their physicochemical features and protein abundances. Microstructural results indicated that the OB mantle exhibited numerous myofibril fragments and disordered microstructures after frozen storage compared with DG tissues. Chemical analysis suggested that freezing resulted in a rapid decrease in myofibrillar protein (MP) content, Ca2+-ATPase activity, and total sulfhydryl content, and promoted the increase in carbonyl content of MPs in both OB and DG. While, DG presented better MP stability than OB muscle after 120 days of frozen storage. Label-free proteomic analysis detected 24 down- and 33 up-regulated differentially abundant proteins (DAPs) in OB and DG mantles. Identified DAPs including isocitrate dehydrogenase and malic enzyme initiated a rapid decrease in the MP properties in OB samples. Moreover, DAPs were related to cytoskeleton function, including paramyosin, tropomyosin, and troponin C, which improved the stability of DG in response to freezing-induced changes.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteômica / Proteínas Musculares Limite: Animals Idioma: En Revista: Food Chem Ano de publicação: 2021 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteômica / Proteínas Musculares Limite: Animals Idioma: En Revista: Food Chem Ano de publicação: 2021 Tipo de documento: Article