Application of polymannosylated cystatin to surimi from roe‐herring to prevent gel weakening

Abstract

A recombinant glycosylated cystatin with a polymannosyl chain was added to roe-herring surimi for preventing gel weakening due to autolysis during cooking. Proteolysis of myosin heavy chain in the surimi was effectively suppressed while cooking at 90³C for 20 min after preincubation at 40³C for 30 min. The glycosylation of cystatin improved the stability against heating as well as proteolysis by cathepsin D. This process markedly improved the texture of the cooked surimi gel with gel strength 2.5 times that of unglycosylated control cystatin.z 1998 Federation of European Biochemical Societies.

Glycosylation Modification Improved the Characteristics of Recombinant Chicken Cystatin and Its Application on Mackerel Surimi

“…Despite the additional amount of glycocystatin, which was 2-fold that of recombinant, and the 40 and 15% increases in breaking force and deformation excess, the maximum level of recombinant cystatin gel was also achieved. Nakamura et al (29) reported a similar phenomenon that glycosylated cystatin C markedly improved the gel strength of roe-herring surimi, which was 2.5-fold that of unglycosylated type. As indicated in Figure 5, the disintegration on MHC of 1 unit of both cystatin gels was obviously observed in addition to the control gel, whereas the actin in gel-softening surimi gels still remained intact.…”

Bovine Plasma Protein Functions in Surimi Gelation Compared with Cysteine Protease Inhibitors

“…Auerswald et al (1989) cloned a chicken cystatin gene into E. coli and synthesized the inhibitor as 20% of total cell proteins. With yeast carrying a mouse cystatin C gene, Nakamura et al (1998) produced a recombinant glycosylated cystatin that was more stable than the non-glycosylated form against heating and proteolysis. Tested as an additive to herring surimi, the glycosylated form was reported to improve gel strength 2.5 times over that of the non-glycosylated cystatin form.…”

Degradation of myofibrils in cultured yellowtail Seriola quinqueradiata burnt meat: effects of a myofibril-bound EDTA-sensitive protease

“…Several studies have shown that the different types of endogenous protease, such as cathepsins [12][13][14][15][16], aspartic acid proteases [17] or serine proteinases [18,19], especially the myofibril-bound serine proteinases [20,21], led to the degradation of myofibrillar proteins in fish meat.…”