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L-glycine and L-cysteine exhibit, strong inhibition of partial purified DIPHENOL OXIDASE at strawberry. The concentration of L-glycine inhibiting Diphenol oxidase activity by 50% (IC50) was 0.5 and 0.4 mM at pH 6.7 and 8, respectively. The inhibition of partial purified Diphenol oxidase activity is pH and inhibitor dependent. Kinetic studies indicate that L-glycine is a uncompetetive inhibitor and L-cysteine is competitive and noncompetitive inhibitor of Diphenol oxidase activity. Vmax and Km for catechol oxidation at pH 6.7 and in presence of L-glycine (1.4M) was 0.09 ∆A min-1 and 10 mM. Vmax for catechol oxidation at pH 8 and in absence of L-glycine was 0.09 ∆A min–1, with a Km of 3.5 mM. Kinetics parameters indicated the highest catalytic efficiency ( units mg–1 prot mM–1) with catechol and L-glycine at pH 8: 4 , then with L-cystein at pH 8: 1.7, L-glycine at pH 6.7: 1.4 and L-cystein at pH 6.7: 0.25.
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194--202
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Bibliogr. 15 poz., tab., wykr., wz.
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Bibliografia
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- [10] Ryan, C.A. Biochim. Biophys. Acta . (2000), 1477, 112–121.
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Bibliografia
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bwmeta1.element.baztech-0963137a-ca32-4eb2-83c4-b8f8451118c0