Trypsin Inhibitory Activity and Gel‐Enhancing Effect of Sarcoplasmic Proteins from Common Carp

Abstract

Sarcoplasmic protein from common carp muscle could be used as a functional protein ingredient that minimizes muscle proteolysis and improves textural properties of surimi containing trypsin-like endogenous proteinases.

Impact of sarcoplasmic proteins on texture and color of silver carp and Alaska Pollock protein gels

“…Moreover, it triggers acyl transfer reaction which enables the formation of 3-(g-glutamyl)lysine linkages between molecules that are not susceptible to proteolytic activity (Yongsawatdigul & Piyadhammaviboon, 2007). Sarcoplasmic protein isolated from common carp also showed proteolysis inhibitory activity and incorporation of 1.8 g sarcoplasmic protein/kg paste into Threadfin bream surimi gels increased gel breaking force and resistance to deformation by inhibiting proteolysis (Siriangkanakun & Yongsawatdigul, 2012). Texture profile analysis (TPA) results presented in Fig.…”

“…Lightness of the SC gels were statistically higher (p < 0.05) when sarcoplasmic proteins and TGase were added. This may be due to the proteolytic activity inhibition effect of sarcoplasmic proteins lowering gel darkening and the increased protein binding caused by exogenous TGase addition working synergistically to form a homogenous inner gel network (Siriangkanakun & Yongsawatdigul, 2012).…”

Antioxidant, Liver Protective and Angiotensin I-converting Enzyme Inhibitory Activities of Old Laying Hen Hydrolysate in Crab Meat Analogue

“…Enzyme hydrolysis improves the nutritional and functional properties of proteins, and has been proposed for proteins from residual sources (Moure et al, 2006). In addition, protein hydrolysates from animal byproducts have been found to exhibit antioxidant activity and improved functional properties (Saiga et al, 2003; Siriangkanakun and Yongsawatdigul, 2012). In particular, peptides have been shown to exert antioxidant, antimicrobial, and antihypertensive activities (Saiga et al, 2003; Jang et al, 2008; Liu et al, 2009; Escudero et al, 2010).…”

Identification by GeLC‐MS/MS of Trypsin Inhibitor in Sarcoplasmic Proteins of Three Tropical Fish and Characterization of Their Inhibitory Properties

“…Gel‐enhancing effect of fish sarcoplasmic proteins has been attributed to various factors, including residual endogenous transglutaminase (Yongsawatdigul and Piyadhammaviboon ) and the presence of protein(s) with gel‐forming ability (Morioka and others ). In addition, endogenous proteinase inhibitor in sarcoplasmic proteins has been reported to be a key factor improving myofibrillar protein gelation (Siriangkanakun and Yongsawatdigul ). Therefore, sarcoplasmic protein might be an alternative ingredient for controlling proteolysis of proteinase‐laden muscle proteins.…”

“…Therefore, sarcoplasmic protein might be an alternative ingredient for controlling proteolysis of proteinase‐laden muscle proteins. Endogenous muscular proteinase inhibitors have been reported in freshwater fish including common carp and crucian carp (Sun and others ; Siriangkanakun and Yongsawatdigul ). However, there is limited information on endogenous proteinase inhibitors in marine fish species that are economically important to seafood industry, particularly threadfin bream ( Nemipterus spp.…”