The effects of sodium chloride on proteins aggregation, conformation and gel properties of pork myofibrillar protein Run
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ORIGINAL ARTICLE
The effects of sodium chloride on proteins aggregation, conformation and gel properties of pork myofibrillar protein Running Head: Relationship aggregation, conformation and gel properties Zhuang-Li Kang1 • Xue-hua Zhang1 • Xiang Li1 • Zhao-jun Song1 • Han-jun Ma1 • Fei Lu1 • Ming-ming Zhu1 • Sheng-ming zhao1 • Zheng-rong Wang1
Revised: 7 June 2020 / Accepted: 13 August 2020 Ó Association of Food Scientists & Technologists (India) 2020
Abstract The objective of this study was to evaluate relationship with aggregation, secondary structures and gel properties of pork myofibrillar protein with different sodium chloride (1%, 2% and 3%). When the sodium chloride increased from 1 to 3%, the active sulfhydryl, surface hydrophobicity, hardness and cooking yield of myofibrillar protein were increased significantly (p \ 0.05), the particle size, total sulfhydryl and Zeta potential were decreased significantly (p \ 0.05), these meant the aggregations of pork myofibrillar protein were decreased. The changes of proteins aggregation induced the strongest intensity band of Amide I shifted up from 1660 cm-1 to 1661 cm-1, meanwhile, the b-sheet structure content was increased significantly (p \ 0.05) with the sodium chloride increased. From the above, the lower proteins aggregation and higher b-sheet structure content could improve the water holding capacity and texture of pork myofibrillar protein gel. Keywords Myofibrillar Sodium chloride Aggregation Texture Gel properties
Introduction Myofibrillar protein accounts for 50–55% of the total protein content of muscle, mainly composes of myosin and actin, which is the main function of the protein in processing, and the changes of the structure and conformation & Zhuang-Li Kang [email protected] 1
School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, People’s Republic of China
of the myofibrillar protein are largely affected the textural and structural properties of meat and meat products (Zhang et al. 2017a, b; Shen et al. 2019a, b; Li et al. 2020a, b). The formation of heat-induced myofibrillar protein gel needed to undergo three processes, such as degeneration, aggregation and cross-linking. The first is non-covalent bond dissociation causes by heating the proteins, then altering the conformation of proteins, causing denaturation of proteins and forming a larger molecule of gel by crosslinking and aggregation (Feng et al. 2017; Guo and Xiong 2019). Sodium chloride played an important role in emulsion meat products, which promoted dissolution and swelling of myofibrillar protein, improved the water holding capacity and oil-preserving performance of the gel, enhanced yield, texture and shelf life of the meat products (Zhang et al., 2017a, b; Paula et al., 2019). In addition, sodium chloride affected protein aggregation, such as soy protein accelerate the aggregation rate after adding sodium chloride, the degree of hydrolysis unchanged, which was due to rapid increase of short-chain elastin after heated (Marı´n, Alema´n et a
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