Contribution of the polymerization of protein by disulfide bonding to increased gel strength of walleye pollack surimi gel with preheating time

Abstract

ABSTRACT:To clarify the contribution of polymerization of myosin heavy chain (MHC) by disulfide bonding to increased gel strength of cooked gel via preheating, the pastes of walleye pollack surimi (SS and C grades) were preheated at 25∞C and 40∞C for a variety of hours prior to heating at 80∞C for 20 min. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) patterns of cooked gels were analyzed with and without reducing the samples, which were solubilized in 8 M urea-2% SDS solution. The formation of polymers by disulfide bonding in cooked gels was almost constant in each of the SS and C grade surimi gels despite the period of preheating. Therefore, it was suggested that polymerization by disulfide bonding occurred during cooking at 80∞C and not during preheating.KEY WORDS: disulfide bond, gel formation, myosin heavy chain, suwari, walleye pollack surimi.

Effects of Rice-related Products on the Textural Properties and Color of Fish Meat Gels Derived from Walleye Pollock (Theragra chalcagramma)

“…The breaking strains of the gel samples containing rice flour at 50℃ and rice bran at 60℃ were significantly higher compared with those containing rice starch and those without additives at the same temperatures. The proteases found in fish muscle are commonly active at 50℃ − 60℃, which can lead to gel structure disintegration or softening (modori) due to the degradation of myofibrillar proteins Hossain et al, 2001a). However, the myosin heavy chain degradation in walleye pollock surimi is due to proteases with different active sites, as this degradation is inhibited by various serine protease inhibitors and cysteine protease inhibitors (Hamann et al, 1990;Hossain et al, 2001b;Hu et al, 2007).…”

“…The proteases found in fish muscles are commonly active at 50℃ − 60℃ and can cause rapid and severe degradation of myofibrillar proteins, particularly myosin heavy chain . This phenomenon, which is known as "modori," lowers the gel strength Hossain et al, 2001a). In contrast, deterioration in the quality of fish meat gel can also be suppressed by various food grade protease inhibitors (Hamann et al, 1990;Morrissey et al, 1993).…”

“…In general, the gel with cooking at 50℃ − 60℃ had the most inferior textural properties (modori phenomenon) (Shimizu et al, 1981;Hossain et al, 2001a). Gelatinization of starch during cooking increases the elasticity of fish meat gel (Yamazawa, 1990).…”

Effect of Rainbow Trout (Oncorhynchus mykiss) Plasma Protein on the Gelation of Alaska Pollock (Theragra chalcogramma) Surimi

“…Disulfide bonds are the only covalent cross‐links found naturally in proteins, and help to stabilize the folded structure (Benjakul and Visessanguan 2000). The polymerization by disulfide bonding of Alaska pollock surimi occurred only during cooking at temperatures higher than 80 °C and not during preheating (Hossain and others 2001). Protein solubility of modori gel decreased as the addition amount of RPP increased up to 0.75 mg/g ( P < 0.05).…”

Classification of Surimi Gel Strength Patterns Using Backpropagation Neural Network and Principal Component Analysis

“…This is because the setting at low temperature prior to heating at a higher temperature allows slow ordering of the protein molecule resulting in good gelation, fine structure and great elasticity [6] [8]. Different temperatures in the setting step result in different conformation of the proteins leading to different structure, and strength of the final gel [7].…”