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内源性蛋白酶对海湾扇贝(Argopecten irradians)闭壳肌冷藏期间质地劣化的作用及其机制。

Action of endogenous proteases on texture deterioration of the bay scallop (Argopecten irradians) adductor muscle during cold storage and its mechanism.

作者信息

Liu Bing, Liu Zi-Qiang, Li De-Yang, Yu Man-Man, Liu Yu-Xin, Qin Lei, Zhou Da-Yong, Shahidi Fereidoon, Zhu Bei-Wei

机构信息

School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, PR China; National Engineering Research Center of Seafood, Dalian 116034, PR China.

School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, PR China.

出版信息

Food Chem. 2020 Apr 11;323:126790. doi: 10.1016/j.foodchem.2020.126790.

DOI:10.1016/j.foodchem.2020.126790
PMID:32305808
Abstract

Texture deterioration occurs in adductor muscle of scallop (Argopecten irradians) (AMS) after 5 d of cold storage. Principal component analysis indicated the texture deterioration resulted in significant decrease of hardness, springiness, adhesiveness and chewiness, but significantly increased cohesiveness. Endogenous proteases degraded structural proteins, among which cysteine proteases were mainly responsible for myofibrillar proteins (MPs) degradation, while serine proteases degraded both MPs and connective tissue proteins. Pearson coefficient analysis showed that texture indicators significantly correlated with structural protein indicators in AMS. To be more specific, the hardness, springiness, adhesiveness and chewiness negatively correlated with myofibrillar fragmentation index, soluble hydroxyproline (Hyp) and soluble glycosaminoglycans, but positively correlated with solubility of MPs and water holding capacity. Meanwhile, the cohesiveness positively correlated with soluble Hyp. The Taylor diagram and Hierarchical cluster analysis confirmed that the inhibitors of cysteine and serine proteases could effectively retard textural deterioration of AMS during 5 d of cold storage.

摘要

冷藏5天后,扇贝(海湾扇贝)闭壳肌(AMS)出现质地劣化。主成分分析表明,质地劣化导致硬度、弹性、黏附性和咀嚼性显著降低,但内聚性显著增加。内源性蛋白酶降解结构蛋白,其中半胱氨酸蛋白酶主要负责肌原纤维蛋白(MPs)的降解,而丝氨酸蛋白酶则降解MPs和结缔组织蛋白。Pearson系数分析表明,质地指标与AMS中的结构蛋白指标显著相关。更具体地说,硬度、弹性、黏附性和咀嚼性与肌原纤维破碎指数、可溶性羟脯氨酸(Hyp)和可溶性糖胺聚糖呈负相关,但与MPs的溶解度和持水能力呈正相关。同时,内聚性与可溶性Hyp呈正相关。泰勒图和层次聚类分析证实,半胱氨酸和丝氨酸蛋白酶抑制剂可有效延缓冷藏5天期间AMS的质地劣化。

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