Surface Modification on Homodimeric Creatinase by Poly-Lysine Binding

doi:10.3969/j.issn.1673-1689.2019.07.019

Home > Archive>Volume 38, Issue 7, 2019 >134-140. DOI:10.3969/j.issn.1673-1689.2019.07.019

Surface Modification on Homodimeric Creatinase by Poly-Lysine Binding
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                        10.3969/j.issn.1673-1689.2019.07.019
                    
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The surface modification of homodimeric creatinase by poly-lysine was carried out to study the effect of enhancing enzyme stability. The influences of different modification condition on enzyme catalytic efficiency and stability were studied by L9（34）orthogonal experiment， the optimal condition were set as molar ratios of CRE-COOH to poly-lysine-NH2 and CRE-COOH to EDC were 1∶100 and 1∶10， in pH 7.0. The covalently binding of poly-lysine onto enzyme surface was tested by SDS-PAGE. The catalytic kinetic parameters （Km and kcat） of modified enzyme were determined as 4.75×10^-5 mol/L and 2.50×10² S^-1， respectively. Moreover， compared to the native enzyme， the thermal and pH stabilities of the modified creatinase were improved， as Tm of modified enzyme was raised by 2.07 ℃， and more than 50% of initial activity of modified enzyme was maintained at pH 4.0 and 10.0， but the control sample was almost no activity. After further exploitation， poly-lysine modification would be one of the effective methods for improving stability of homodimeric creatinase.

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GAO Yanan, XIN Yu, ZHANG Ling, YANG Hailin, WANG Wu. Surface Modification on Homodimeric Creatinase by Poly-Lysine Binding[J]. Journal of Food Science and Biotechnology,2019,38(7):134-140.

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Online: January 23,2020
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