Abstract
The recombinant and glycosylation chicken cystatins were expressed and secreted in the broth of Pichia pastoris X-33 transformant with apparent molecular masses (M) of 14 and 55 kDa, respectively. The glycosylation cystatin (glycocystatin) contained a polysaccharide chain that was composed of 50 DP of mannose residues. Because of the polymannosyl chain, the inhibitory ability in glycocystatin was 90.8% of recombinant cystatin. In addition to freeze-thawing stability, the thermal and pH stabilities as well as the susceptibility of glycocystatin were also enhanced. Both cystatins could improve the mackerel surimi gel by inhibiting the gel softening, which was derived from the hydrolysis of catheptic cysteine proteinases. Despite the additional amount of glycocystatin (8 units), twice that of recombinant cystatin, the 40 and 15% increases in breaking force and deformation of gels were also observed. Accordingly, the surimi gel was further improved by enhancing the stability of chicken cystatin.
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