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首页> 外文期刊>Ukrainian Biochemical Journal >The influence of coordinative tartrate and malatogermanate compounds on the activity of α-L-rhamnosidase preparations from Penicillium tardum, Eupenicillium erubescens and Cryptococcus albidus
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The influence of coordinative tartrate and malatogermanate compounds on the activity of α-L-rhamnosidase preparations from Penicillium tardum, Eupenicillium erubescens and Cryptococcus albidus

机译：双酒石酸和马尔替金属化合物对青霉蛋白，Eupenicillium，Erubeccens和Cryptococcus Assidus的α-L- rhamnosidase制剂活性的影响

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摘要

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)sub3/sub]sub4/sub[{Gesub2/sub(OH)sub2/sub(Tart)sub2/sub}sub3/subClsub2/sub]·15Hsub2/sub on P. tardum α-L-rhamnosidase was revealed. All studied compounds except [CuCl(phen)sub2/sub][Ge(OH)(HMal)sub2/sub] 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.
机译：最近酶的微生物来源的制剂在不同的行业中越来越重要。 α-L- rhamnosidase的制剂用于制药行业以及科学工作作为分析研究的工具。我们已经获得了来自青霉芽孢菌，伊芙尼霉菌的β-L-犀牛酶制剂，Eupenicillium，eupenciruliumens和Cryptococcus albidus微生物菌株是有效的酶生产商。该研究的目的是估计锗配位化合物增强酶催化活性的能力。在0.5和24下，研究了110℃和0.1％浓度在0.01和0.1％浓度上为0.05和24的α-LAdumcens和Cryptococccus 1001的α-L-鼠李糖苷酶制剂的浓度的影响。 ？H阐述。 [Ni（Bipy） 3 ] 4 （oh） 2 （馅饼的抑制作用） 2 } 3 cl 2 ]·15h 2 在p.tardumα-l-rhamnosidase上被揭示。除了[CuCl（Phen） 2 ]外，所有研究的化合物显示出在塔TARDUMα-L-rhamnosidase的活性增加更长的博览会。 E.E.Subescensα-L- rhamnosidase的活性被显示为可由D-金属阳离子化合物刺激。对于所研究的所有化合物，Asbidusα-L- rhamnosid酶发生不敏感。

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