O. Gudzenko, N. Borzova, L. Varbanets, I. Seifullina, E. Afanasenko, E.V. Martsinko
{"title":"超分子三维金属1,10-菲罗啉酒石酸盐(IV)对隐球菌、绿绿青霉和限制青霉α- l -鼠李糖苷酶活性的影响","authors":"O. Gudzenko, N. Borzova, L. Varbanets, I. Seifullina, E. Afanasenko, E.V. Martsinko","doi":"10.15407/microbiolj84.05.003","DOIUrl":null,"url":null,"abstract":"In recent years, the particular interest of researchers is focused on such enzymes as α-L-rhamnosidase and α-galactosidase. These enzymes are considered useful for various applications. α-L-rhamnosidases may be applied for debittering of citrus fruit juices, due to the less bitter taste of the derhamnosylated flavonones, for rhamnose production, and for the determination of the anomeric configuration in polysaccharides, glycosides and glycolipids. These enzymes may enhance wine aroma and flavonoid bioavailability, or assist in the synthesis of pharmaceuticals. α-Galactosidase finds application in many areas. It is widely used in the food industry to improve the quality of soy products by hydrolyzing indigestible galactosides such as raffinose and stachyose, in the processing of raw materials in order to increase the yield of sugar from molasses, and for the biotransformation of human blood erythrocytes of group B (III) in universal donor erythrocytes, as well as in enzyme therapy of some congenital disorders of sphingolipid metabolism. Earlier, as a result of screening microorganisms of different taxonomic groups, we has selected active α-L-rhamnosidase and α-galactosidase producers. One way to increase their activity is using various effector compounds capable of modifying the enzyme activity. The study of the influence of various effectors is one of the priority areas of modern research in biochemistry, biocoordination chemistry, and biotechnology. Recent advantages in the area of biocoordination chemistry revealed high activating properties of double heterometallic mixed-ligand coor dination compounds with germanium(IV)/tin(IV) tartaric complex anions and 1,10-phenanthroline/2,2`-bipyridine d-metallic cations. The aim is to estimate the enzyme-effector activity of five similar tartratostannates for the α-L-rhamnosidases of Cryptococcus albidus, Eupenicillium erubescens, and α-galactosidase of Penicillium restrictum. Methods. The activity of α-Galactosidase was determined using p-nitrophenyl-α-D-galactopyranoside («Sigma», USA) as a substrate. The activity of α-L-rhamnosidase was determined using the Davis method. As modifiers of enzyme activity, [Fe(phen)3]2[Sn2(μ-Tart)2(Н2Tart)2]·2H2O (1), [Co(phen)3]2[Sn2(μ-Tart)2(Н2Tart)2]·8H2O (2), [Ni(phen)3]2[Sn2(μ-Tart)2(Н2Tart)2]·2H2O (3), [Cu(phen)3]2[Sn2(μ-Tart)2(Н2Tart)2]·2H2O (4), and [Zn(phen)3]2[Sn2(μ-Tart)2(Н2Tart)2]·6H2O (5) were used. Results. The study of the effect of complexes 1—5, which are supramolecular salts consisting of the same tartrate stannate anion (electrophilic agent) and a 1,10-phenanthroline d-metal cation (nucleophilic agent), on the Cryptococcus albidus, Eupenicillium erubescens α-L-rhamnosidases, and Penicillium restrictum α-galactosidase showed that the compounds tested had a different influence on the enzymes’ activity. The catalytic activity of α-L-rhamnosidase is significantly influenced by all complexes. The effectiveness of compounds 1—5 for P. restrictum α-galactosidase was less pronounced in comparison with C. albidus and E. erubescens α-L-rhamnosidases. It was mostly at the control level. There was observed a certain pattern in the influence of complexes on α-L-rhamnosidases of Cryptococcus albidus and Eupenicillium erubescens. Compounds 2 and 5 turned out to be the most effective and activated enzymes by 500-900%. Conclusions. Compound 2 [Co(phen)3]2[Sn2(μ-Tart)2(Н2Tart)2]·8H2O is promising for further use as an effector of the α-L-rhamnosidase activity.","PeriodicalId":18628,"journal":{"name":"Mikrobiolohichnyi zhurnal","volume":"53 4","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2023-02-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Supramolecular 3-d Metal 1,10-Phenanthroline Tartratostannates(IV) as Modifiers of α-L-Rhamnosidase Activity of Cryptococcus albidus, Eupenicillium erubescens and α-Galactosidase Activity of Penicillium restrictum\",\"authors\":\"O. Gudzenko, N. Borzova, L. Varbanets, I. Seifullina, E. Afanasenko, E.V. Martsinko\",\"doi\":\"10.15407/microbiolj84.05.003\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"In recent years, the particular interest of researchers is focused on such enzymes as α-L-rhamnosidase and α-galactosidase. These enzymes are considered useful for various applications. α-L-rhamnosidases may be applied for debittering of citrus fruit juices, due to the less bitter taste of the derhamnosylated flavonones, for rhamnose production, and for the determination of the anomeric configuration in polysaccharides, glycosides and glycolipids. These enzymes may enhance wine aroma and flavonoid bioavailability, or assist in the synthesis of pharmaceuticals. α-Galactosidase finds application in many areas. It is widely used in the food industry to improve the quality of soy products by hydrolyzing indigestible galactosides such as raffinose and stachyose, in the processing of raw materials in order to increase the yield of sugar from molasses, and for the biotransformation of human blood erythrocytes of group B (III) in universal donor erythrocytes, as well as in enzyme therapy of some congenital disorders of sphingolipid metabolism. Earlier, as a result of screening microorganisms of different taxonomic groups, we has selected active α-L-rhamnosidase and α-galactosidase producers. One way to increase their activity is using various effector compounds capable of modifying the enzyme activity. The study of the influence of various effectors is one of the priority areas of modern research in biochemistry, biocoordination chemistry, and biotechnology. Recent advantages in the area of biocoordination chemistry revealed high activating properties of double heterometallic mixed-ligand coor dination compounds with germanium(IV)/tin(IV) tartaric complex anions and 1,10-phenanthroline/2,2`-bipyridine d-metallic cations. The aim is to estimate the enzyme-effector activity of five similar tartratostannates for the α-L-rhamnosidases of Cryptococcus albidus, Eupenicillium erubescens, and α-galactosidase of Penicillium restrictum. Methods. The activity of α-Galactosidase was determined using p-nitrophenyl-α-D-galactopyranoside («Sigma», USA) as a substrate. The activity of α-L-rhamnosidase was determined using the Davis method. As modifiers of enzyme activity, [Fe(phen)3]2[Sn2(μ-Tart)2(Н2Tart)2]·2H2O (1), [Co(phen)3]2[Sn2(μ-Tart)2(Н2Tart)2]·8H2O (2), [Ni(phen)3]2[Sn2(μ-Tart)2(Н2Tart)2]·2H2O (3), [Cu(phen)3]2[Sn2(μ-Tart)2(Н2Tart)2]·2H2O (4), and [Zn(phen)3]2[Sn2(μ-Tart)2(Н2Tart)2]·6H2O (5) were used. Results. The study of the effect of complexes 1—5, which are supramolecular salts consisting of the same tartrate stannate anion (electrophilic agent) and a 1,10-phenanthroline d-metal cation (nucleophilic agent), on the Cryptococcus albidus, Eupenicillium erubescens α-L-rhamnosidases, and Penicillium restrictum α-galactosidase showed that the compounds tested had a different influence on the enzymes’ activity. The catalytic activity of α-L-rhamnosidase is significantly influenced by all complexes. The effectiveness of compounds 1—5 for P. restrictum α-galactosidase was less pronounced in comparison with C. albidus and E. erubescens α-L-rhamnosidases. It was mostly at the control level. There was observed a certain pattern in the influence of complexes on α-L-rhamnosidases of Cryptococcus albidus and Eupenicillium erubescens. Compounds 2 and 5 turned out to be the most effective and activated enzymes by 500-900%. Conclusions. Compound 2 [Co(phen)3]2[Sn2(μ-Tart)2(Н2Tart)2]·8H2O is promising for further use as an effector of the α-L-rhamnosidase activity.\",\"PeriodicalId\":18628,\"journal\":{\"name\":\"Mikrobiolohichnyi zhurnal\",\"volume\":\"53 4\",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2023-02-17\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Mikrobiolohichnyi zhurnal\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.15407/microbiolj84.05.003\",\"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":"Mikrobiolohichnyi zhurnal","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.15407/microbiolj84.05.003","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}
引用次数: 0
摘要
近年来,研究人员特别关注α- l -鼠李糖酶和α-半乳糖苷酶等酶。这些酶被认为对各种应用都很有用。α- l -鼠李糖苷酶可用于柑桔果汁的脱臭,因为鼠李糖化黄酮的苦味较小,也可用于鼠李糖的生产,并可用于测定多糖、糖苷和糖脂中的头聚糖构型。这些酶可以提高葡萄酒的香气和类黄酮的生物利用度,或协助药物的合成。α-半乳糖苷酶在许多领域都有应用。它广泛应用于食品工业,通过水解棉子糖和水苏糖等难消化的半乳糖苷来提高豆制品的质量,用于原料加工以提高糖蜜的糖产量,用于人血液B (III)族红细胞在通用供体红细胞中的生物转化,以及用于一些先天性鞘脂代谢障碍的酶治疗。在此之前,通过对不同分类群微生物的筛选,我们筛选出了α- l -鼠李糖苷酶活性菌和α-半乳糖苷酶活性菌。增加其活性的一种方法是使用能够修饰酶活性的各种效应化合物。研究各种效应物的影响是生物化学、生物配位化学和生物技术现代研究的重点领域之一。锗(IV)/锡(IV)酒石酸配合物阴离子和1,10-菲罗啉/2,2′-联吡啶金属阳离子的双杂金属混合配体配合物具有较高的活化性能,是近年来生物配位化学领域的研究热点。目的是估计五种相似的酒石酸盐对隐球菌、绿绿青霉和限制青霉α- l -鼠李糖苷酶的酶效活性。方法。α-半乳糖苷酶的活性以对硝基苯-α- d -半乳糖苷(Sigma, USA)为底物测定。采用Davis法测定α- l -鼠李糖苷酶活性。作为酶活性的修饰符,[Fe(苯酚的)3]2 [Sn2(μ馅饼)2(Н2馅饼)2)·2水(1),[有限公司(苯酚的)3]2 [Sn2(μ馅饼)2(Н2馅饼)2)8·h2o (2), (Ni(苯酚的)3]2 [Sn2(μ馅饼)2(Н2馅饼)2)·2水(3),[铜(苯酚的)3]2 [Sn2(μ馅饼)2(Н2馅饼)2)·2水(4),和[锌(苯酚的)3]2 [Sn2(μ馅饼)2(Н2馅饼)2)6·h2o(5)。结果。由酒石酸盐、锡酸盐阴离子(亲电剂)和1,10-菲罗啉d-金属阳离子(亲核剂)组成的超分子盐类配合物1 - 5对隐球菌、绿绿青霉α- l -鼠李糖酶和限制性青霉α-半乳糖苷酶活性的影响研究表明,所测化合物对这些酶的活性有不同的影响。α- l -鼠李糖苷酶的催化活性受到各配合物的显著影响。化合物1 ~ 5对限制草α-半乳糖糖苷酶的抑制作用较差,而对杜鹃α- l -鼠李糖糖苷酶的抑制作用较差。它主要是在控制水平。配合物对隐球菌α- l -鼠李糖苷酶的影响有一定的规律。化合物2和5是最有效的酶,激活率为500-900%。结论。化合物2[Co(phen)3]2[Sn2(μ-Tart)2(Н2Tart)2]·8H2O作为α- l -鼠李糖苷酶活性的影响因子有进一步的应用前景。
Supramolecular 3-d Metal 1,10-Phenanthroline Tartratostannates(IV) as Modifiers of α-L-Rhamnosidase Activity of Cryptococcus albidus, Eupenicillium erubescens and α-Galactosidase Activity of Penicillium restrictum
In recent years, the particular interest of researchers is focused on such enzymes as α-L-rhamnosidase and α-galactosidase. These enzymes are considered useful for various applications. α-L-rhamnosidases may be applied for debittering of citrus fruit juices, due to the less bitter taste of the derhamnosylated flavonones, for rhamnose production, and for the determination of the anomeric configuration in polysaccharides, glycosides and glycolipids. These enzymes may enhance wine aroma and flavonoid bioavailability, or assist in the synthesis of pharmaceuticals. α-Galactosidase finds application in many areas. It is widely used in the food industry to improve the quality of soy products by hydrolyzing indigestible galactosides such as raffinose and stachyose, in the processing of raw materials in order to increase the yield of sugar from molasses, and for the biotransformation of human blood erythrocytes of group B (III) in universal donor erythrocytes, as well as in enzyme therapy of some congenital disorders of sphingolipid metabolism. Earlier, as a result of screening microorganisms of different taxonomic groups, we has selected active α-L-rhamnosidase and α-galactosidase producers. One way to increase their activity is using various effector compounds capable of modifying the enzyme activity. The study of the influence of various effectors is one of the priority areas of modern research in biochemistry, biocoordination chemistry, and biotechnology. Recent advantages in the area of biocoordination chemistry revealed high activating properties of double heterometallic mixed-ligand coor dination compounds with germanium(IV)/tin(IV) tartaric complex anions and 1,10-phenanthroline/2,2`-bipyridine d-metallic cations. The aim is to estimate the enzyme-effector activity of five similar tartratostannates for the α-L-rhamnosidases of Cryptococcus albidus, Eupenicillium erubescens, and α-galactosidase of Penicillium restrictum. Methods. The activity of α-Galactosidase was determined using p-nitrophenyl-α-D-galactopyranoside («Sigma», USA) as a substrate. The activity of α-L-rhamnosidase was determined using the Davis method. As modifiers of enzyme activity, [Fe(phen)3]2[Sn2(μ-Tart)2(Н2Tart)2]·2H2O (1), [Co(phen)3]2[Sn2(μ-Tart)2(Н2Tart)2]·8H2O (2), [Ni(phen)3]2[Sn2(μ-Tart)2(Н2Tart)2]·2H2O (3), [Cu(phen)3]2[Sn2(μ-Tart)2(Н2Tart)2]·2H2O (4), and [Zn(phen)3]2[Sn2(μ-Tart)2(Н2Tart)2]·6H2O (5) were used. Results. The study of the effect of complexes 1—5, which are supramolecular salts consisting of the same tartrate stannate anion (electrophilic agent) and a 1,10-phenanthroline d-metal cation (nucleophilic agent), on the Cryptococcus albidus, Eupenicillium erubescens α-L-rhamnosidases, and Penicillium restrictum α-galactosidase showed that the compounds tested had a different influence on the enzymes’ activity. The catalytic activity of α-L-rhamnosidase is significantly influenced by all complexes. The effectiveness of compounds 1—5 for P. restrictum α-galactosidase was less pronounced in comparison with C. albidus and E. erubescens α-L-rhamnosidases. It was mostly at the control level. There was observed a certain pattern in the influence of complexes on α-L-rhamnosidases of Cryptococcus albidus and Eupenicillium erubescens. Compounds 2 and 5 turned out to be the most effective and activated enzymes by 500-900%. Conclusions. Compound 2 [Co(phen)3]2[Sn2(μ-Tart)2(Н2Tart)2]·8H2O is promising for further use as an effector of the α-L-rhamnosidase activity.