Effects of Cathepsins on Gel Strength and Water-Holding Capacity of Myofibrillar Protein Gels from Bighead Carp (Aristichthys nobilis) under a Hydroxyl Radical-Generation Oxidizing System.

Han Lu,Gang Wen,Yunhong Liang,Xiangmei Zhang

doi:10.3390/foods11030330

Han Lu, Gang Wen + Show 2 more

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https://doi.org/10.3390/foods11030330

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Abstract

This study investigates the effects of cathepsins on the gel strength and water-holding capacity (WHC) of myofibrillar protein gels from bighead carp (Aristichthys nobilis) under a hydroxyl radical-generation oxidizing system. The myofibrillar proteins were divided into control group (with cathepsins) and E64 group (without cathepsins). The changes of cathepsin B and cathepsin L activities, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), protein oxidation (total sulfhydryl and carbonyl contents), and chemical interactions (nonspecific association, ionic bonds, hydrogen bonds, hydrophobic interactions, and disulfides) of myofibrillar protein and gels, as well as the gel strength and WHC of two groups under 0–100 mM H2O2, were measured. The results indicated that mild oxidation (10 mM H2O2) made a better gel strength and WHC. Cathepsin B and L activities decreased with increasing H2O2 concentrations but their effects on myofibrillar protein degradation still existed during 0.1–50 mM H2O2, which was expressed by higher carbonyl contents and ionic bonds at 0.1 and 50 mM H2O2, higher total sulfhydryl contents at 0 mM H2O2, and a lower intensity of MHC and actin of the control group than the E64 group. Besides more protein degradation, cathepsin proteolysis also resulted in lower gel strength and WHC in control gels than E64 gels under mild oxidation, which could be explained by lower hydrophobic interaction and moderate disulfides bonds between gel protein molecules of control gels.

Highlights

Surimi modori is a problem that cannot be ignored in surimi products, which could result in quality deterioration, and eventually have a negative effect on the acceptance and commercial price of the surimi products [1]
There are three reasons for the important role played by endogenous cathepsins on surimi modori: firstly, the cathepsins are myofibril-bound protease and difficult to remove by rinsing during the surimi preparation [6]; secondly, the optical pH value for cathepsin B and L hydrolysis is within the range of postmortem fish; thirdly, the cathepsins are heat-stable and exhibit considerable proteolysis rates, especially at 50–70 ◦C [7], which indicate their possible role in heat-induced surimi gels
This result indicated that cathepsin L had greater effects on protein degradation than cathepsin B, which was reported by Lu et al [33] in chilled and partial frozen bighead carp

Summary

Introduction

Surimi modori is a problem that cannot be ignored in surimi products, which could result in quality deterioration, and eventually have a negative effect on the acceptance and commercial price of the surimi products [1]. Cathepsins, which belong to a large family of lysosomal cysteine proteases, play a major role in protein degradation of postmortem fish muscle [2]. They hydrolyze a broad range of proteins, such as myosin, actin, nebulin, insulin, myoglobin, glucagon, azocasein, histones, haemoglobin, and insoluble collagen [3,4,5]. Hu et al [8] proved that cathepsin L is involved in modori phenomenon by its hydrolysis of the main protein in carp surimi and results in the decreased gel strength

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