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| Makale Dili | – | Basım Tarihi | 07-1998 |
| Makale Linki | https://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/fn107108g | ||
| UAK Araştırma Alanları |
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| Özet |
| High proteolytic activity Pacific whiting muscle causes hydrolysis of myofibrillar protein and lowers surimi gel quality. Although food grade proteinase inhibitors can be used to prevent autolytic activity in surimi, their usage is limited due to their adverse effects on the organoleptic quality of surimi. Cystatins however can be used as a specific cysteine proteinase inhibitor without adverse effects. Recombinant cystatins were characterized for their inhibitory activity against cysteine proteinase and compared to egg white cystatin to develop a specific proteinase inhibitor to be used in Pacific whiting surimi. Soyacystatin expressed in E. Coil was purified with phenyl-Sepharose and DEAE 4.33 fold as a recombinant protein. Recombinant fish cystatin expressed in E. coil was also purified as a recombinant protein by affinity chromatography using Ni-NTA resin. Native egg white cystatin was purified 343 fold by using affinity chromatography on cm-papain-Sepharose. Fish cystatin, soyacystatin and egg white cystatin were tested for their inhibitory activity. The amount required to inhibit 50% activity of 2 [mu] g papain was 0.245 [mu] g and 0.455 [mu] g for soyacystatin and egg white cystatin, respectively. The amount of fish cystatin required to inhibit 90% activity of papain was 3.57 [mu] g while the amount of soyacystatin and egg white cystatin required to inhibit was 0.429 and 0.810 [mu] g, respectively. For the characterization study, the fish cystatin was not tested because of low recovery in the purification process. Also, the harsh chemical treatment and lengthy period required to renature the protein made fish cystatin unfeasible for surimi application. Egg white … |
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