Effects of Heat‐Stable Alakaline Protease Activity of Atlantic Menhaden (Brevootii tyrannus) on Surimi Gels

Abstract

Heat stable protease isolated from the sarcoplasmic fraction of menhaden (Brevoorti tyrannus) muscle tissue was characterized as to optimum temperature and pH against casein substrate and its degradative action on actomyosin and surimi during heating. The optimum conditions for activity were 60°C at a pH of 7.5 to 8.0. Activity dropped off remarkably at temperatures below 45°C or above 70°C and when pH was below 7.0 or above 8.0. The enzyme(s) was capable of degrading actomyosin as observed by sodium dodecyl sulfate electrophoresis. This implicated a causative role for this protease system in the texture degradation observed during thermal processing of menhaden surimi at temperatures of .50-70°C.

Surimi of king weakfish (Macrodon ancylodon) wastes: texture gel evaluation with protease inhibitors and transglutaminase

“…The remaining treatments although significantly better in comparison to control (G1), did not obtain difference themselves (P<0.05). The kamaboko gels from King weakfish surimi without inhibitors (control) have presented high compression force (>2.0 kg) likely to Atlantic menhaden (Brevoortia tyrannus) gels at the same conditions (Boye and Lanier, 1988). The gel strength average of surimi from tilapia (Oreochomis sp) in compression tests reached 1.0kg although using hydrocolloids (Barreto and Beirão, 1999).…”

“…This behavior to the gel formation was also observed in salmon (Salmo salar), which had temperature setting among 40-60ºC by heating up to 30 min (Saeki et al, 1995). Probably by extension of the heating time, besides 30 min, that myofibrillar proteolysis (modori) from King weakfish should be better characterized as such happened in Atlantic menhaden (Brevoortia tyrannus) that presented proteolysis at heating times of 90-120 min for 60°C (Boye and Lanier, 1988).…”

“…The force required for a specified degree of compression of its original length was reported in grams (g); cohesiveness was calculated as the ratio of the peak of the second compression curve to the peak of first compression curve. Samples of kamaboko gels were subjected to compression in ¼ of their original length (axial axes) using a crosshead speed and chart of 10cm.min -1 and a load cell of 50kg (Soares and Arêas, 1995;Boye and Lanier, 1988;Arêas and Lawrie, 1984).…”

Chicken plasma protein: Proteinase inhibitory activity and its effect on surimi gel properties

“…Two major intracellular degradative pathways involve a lysosomal pathway, including cathepsin proteases, and/or a cytosolic calcium-dependent pathway with calpains (Zeece, Woods, Keen, & Reville, 1992). Alkaline proteinases are also implicated in some fish species (Boye & Lanier, 1988;Lin & Lanier, 1980). Recently, Benjakul, Visessanguan, and Leelapongwattana (2003c) reported that heat-activated alkaline proteinase in bigeye snapper played an important role in degradation of muscle protein, especially at 60-65°C.…”

Heat-activated proteolysis in lizardfish (Saurida tumbil) muscle

“…Cysteine proteinase, especially cathepsin L, was reported to contribute to gel softening of Pacific whiting surimi (Seymour, Morrissey, Peters, & An, 1994) and arrowtooth flounder (Viessanguan et al, 2001). Heat stable alkaline proteinases have been reported to cause the degradation of surimi gel (Boye & Lanier, 1988;Toyohara, Nomata, Makinodan, & Shimizu, 1987).…”