Effect of microbial transglutaminase on autolysis and gelation of lizardfish surimi

Abstract

In the absence of microbial transglutaminase (MTGase), the textural properties of lizardfish surimi (Saurida spp) improved when pre-incubated at 4 and 25 • C for 24 and 4 h, respectively. MTGase optimally catalyzed incorporation of monodansylcadaverine (MDC) into surimi at 40 • C. Addition of MTGase appeared to reduce autolytic activity at 25 and 40 • C, but had no effect on autolytic activity at 65 • C. Breaking force and deformation of lizardfish surimi significantly improved when 0.1 unit MTGase g −1 surimi (1.8 g kg −1 ) was added and pre-incubated at either 25 or 40 • C. Textural properties improved concomitant with cross-linked polymers of myosin heavy chain and tropomyosin, but not actin. Addition of MTGase also improved the storage modulus (G ). The gel network of surimi mixed with MTGase and pre-incubated at 40 • C readily formed during the pre-incubation period, while formation of the gel network began at 48.1 • C in the absence of MTGase.

Properties of surimi gel as influenced by fish gelatin and microbial transglutaminase

“…MTGase played the role in the cross-linking of golden threadfin bream and pollack actomyosin as indicated by gradual decrease in MHC band. Yongsawatdigul and Piyadhammaviboon (2005) reported that protein crosslinking in lizardfish surimi was catalyzed by MTGase at 40 1C for 1 h prior to heating at 90 1C for 30 min. It was noted that MHC and actin bands of surimi gel added with fish gelatin decreased as the gelatin level added increased.…”

Modification of functional quality of raw myofibril preparation obtained from water-washed mechanically recovered chicken meat

“…No decrease was found in the percentage share of actin. It is hypothesised that-similarly to the action of heat on proteins-transglutaminase causes changes by a partial development of polypeptide chains and as a consequence in an enhanced availability of hydrophobic fragments [29]. However, in other fragments of the chain protein molecules undergo aggregation, combined with a reduction in availability of hydrophobic fragments and a loss of solubility [30].…”

Color improvement by titanium dioxide and its effect on gelation and texture of proteins recovered from whole fish using isoelectric solubilization/precipitation

“…However, the proteolysis can be inhibited by beef plasma protein (BPP) and others (Kang & Lanier, 2005;Morrissey, Wu, Lin, & An, 1993;Park, Yongsawatdigul, & Lin, 1994). Transglutaminase (TGase) added and also present in fish muscle (i.e., endogenous TGase) results in higher texture quality (Folk, 1980;Park, 2005;Takeda & Seki, 1996;Yongsawatdigul & Piyadhammaviboon, 2005;Yongsawatdigul, Worratao, & Park, 2002). Potato starch (PS) is typically added to fish products because of gelatinization (Park, 2005).…”