Ukr.Biochem.J. 2020; Volume 92, Issue 4, Jul-Aug, pp. 85-95

doi: https://doi.org/10.15407/ubj92.04.085

The influence of coordinative tartrate and malatogermanate compounds on the activity of α-L-rhamnosidase preparations from Penicillium tardum, Eupenicillium erubescens and Cryptococcus albidus

07.09.2020   Uncategorized   No comments

О. V. Gudzenko1, L. D. Varbanets1*, І. I. Seifullina2,
E. А. Chebanenko2, E. Е. Martsinko2, Е. V. Аfanasenko2

1Zabolotny Institute of Microbiology and Virology, National Academy of Sciences of Ukraine, Kyiv;
2Mechnikov Odessa National State University, Ukraine;
*e-mail: varbanets_imv@ukr.net

Received: 26 November 2019; Accepted: 15 May 2020

Recently enzyme preparations of microbial origin become increasingly important in different industries. Preparations of α-L-rhamnosidase are used in the pharmaceutical industry as well as in scientific work as a tool for analytical research. We have obtained purified α-L-rhamnosidase preparations from Penicillium tardum, Eupenicillium erubescens and Cryptococcus albidus microorganism strains which are effective enzyme producers. The aim of the study was to estimate the ability of germanium coordination compounds to enhance enzyme catalytic activity. The effects of 11 heterometal mixed ligand tartrate (malate-)germanate compounds at 0.01 and 0.1% concentration on the activity of α-L-rhamnosidase preparations from Penicillium tardum IMV F-100074, Eupenicillium erubescens and Cryptococcus albidus 1001 were studied at 0.5 and 24 h exposition. The inhibitory effect of [Ni(bipy)3]4[{Ge2(OH)2(Tart)2}3Cl2]·15H2 on P. tardum α-L-rhamnosidase was revealed. All studied compounds except [CuCl(phen)2][Ge(OH)(HMal)2] were shown to increase activity of P. tardum α-L-rhamnosidase at a longer term of exposition. Activity of E. erubescens α-L-rhamnosidase was shown to be stimulated by d-metal cation-free compounds. C. albidus α-L-rhamnosidase occurred to be insensitive to all compounds studied.

Keywords: , , , ,

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