{"title":"酒石酸盐和苹果果酸盐配位化合物对延迟青霉、绿青霉和白隐球菌制备的- l -鼠李糖苷酶活性的影响","authors":"О. V. Gudzenko, L. Varbanets, І. I. Seifullina","doi":"10.15407/ubj92.04.085","DOIUrl":null,"url":null,"abstract":"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.","PeriodicalId":23448,"journal":{"name":"Ukrainian Biochemical Journal","volume":"92 1","pages":"85-95"},"PeriodicalIF":0.0000,"publicationDate":"2020-09-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"6","resultStr":"{\"title\":\"The influence of coordinative tartrate and malatogermanate compounds on the activity of ?-L-rhamnosidase preparations from Penicillium tardum, Eupenicillium erubescens and Cryptococcus albidus\",\"authors\":\"О. V. Gudzenko, L. Varbanets, І. I. Seifullina\",\"doi\":\"10.15407/ubj92.04.085\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"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.\",\"PeriodicalId\":23448,\"journal\":{\"name\":\"Ukrainian Biochemical Journal\",\"volume\":\"92 1\",\"pages\":\"85-95\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2020-09-10\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"6\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Ukrainian Biochemical Journal\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.15407/ubj92.04.085\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"Biochemistry, Genetics and Molecular Biology\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Ukrainian Biochemical Journal","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.15407/ubj92.04.085","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"Biochemistry, Genetics and Molecular Biology","Score":null,"Total":0}
The influence of coordinative tartrate and malatogermanate compounds on the activity of ?-L-rhamnosidase preparations from Penicillium tardum, Eupenicillium erubescens and Cryptococcus albidus
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.
期刊介绍:
The Ukrainian Biochemical Journal publishes original research papers, reviews and brief notes; papers on research methods and techniques; articles on the history of biochemistry, its development and prominent figures; discussion articles; book reviews; chronicles; etc. The journal scope includes not only biochemistry but also related sciences, such as cellular and molecular biology, bioorganic chemistry, biophysics, pharmacology, genetics, and medicine (medical biochemistry et al.) – insofar as the studies use biochemical methods and discuss biochemical findings.