Thermophilic Fungi with Glucosidase and Proteolytic Activities

Borzova, N.V.; Гудзенко, О.В.; Avdiyuk, K.V.; Varbanets, L.D.; Nakonechna, L.T.

doi:10.15407/microbiolj83.03.024

Cited by 4 publications

(3 citation statements)

References 31 publications

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“…Earlier [5,6], we isolated a number of active producers of α-L-rhamnosidases. But since the enzymes of diff erent producers are characterized by various properties, it is necessary to search for new producers of α-L-rhamnosidases, as well as to study the infl uence of a number of synthetic compounds on their activity.…”

Section: ][Ge(hcit) 2 ]•3h 2 O (1); [Ni(phen) 3 ][Ge(hcit) 2 ]•2h 2 O...mentioning

confidence: 99%

Influence of New Types of Biscitratogermanates on Penicillium restrictum α-L-Rhamnosidase

et al. 2023

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The intensive development of biotechnology in the last decade is largely determined by the growing requirement needs of both medicine and various industries for products of microbial synthesis, including glycosidases, in particular α-L-rhamnosidases. Their wide use to solve current biological-medical and chemical-technological problems stimulates researchers to search for compounds capable of influencing their catalytic activity. Therefore, the purpose of this work was to isolate and purify α-L-rhamnosidase from a new producer of Penicillium restrictum and to investigate multi-ligand germanium-3d-metal complexes with citric acid, phenanthroline, and bipyridine as effectors of its activity. Methods. The object of the study was α-L-rhamnosidase of P. restrictum. Its purification was carried out by gel filtration and ion exchange chromatography on TSK-gels and Sepharose 6B. The activity of α-L-rhamnosidase was determined using the Davis method with naringin as a substrate. As modifiers of enzyme activity, purposefully synthesized multiligand germanium-3d-metal complexes with citric acid, phenanthroline, and bipyridine ([Ni(bipy)3][Ge(HCit)2]·3H2O (1); [Ni(phen)3][Ge(HCit)2]·2H2O (2); [{Cu(bipy)2}2Ge(m-Cit)2]·12Н2О (3); [{Cu(phen)2}2Ge(m-Cit)2]·13H2O (4); [Zn(bipy)3][Ge(HCit)2]·2H2O (5); [Zn(phen)3][Ge(HCit)2]·3H2O (6)), were used. Results. From the supernatant of culture fluid of P. restrictum, α-L-rhamnosidase was isolated and purified 23.1 times with a yield of 0.09%. The specific activity of the enzyme was 27.8 units/mL. The enzyme was homogeneous according to gel filtration on Sepharose 6B and had a molecular mass of 50 kDa. It was established that the considered coordination compounds are able to regulate the catalytic activity of α-L-rhamnosidase of P. restrictum. All of them manifest themselves either as activators or as inert substances, no inhibition was observed. In addition, the dependence of the degree of enzyme activation by the compounds on their concentration is traced and corresponds to the following series: at a concentration of 0.01% — 1 > 6 ≈ 5 > 3 >2 ≈ 4 and at a concentration of 0.1% — 1 > 4 > 2 > 5 ≈ 6. 3. The catalytic activity is also significantly affected by the time of exposure to the compounds: at a concentration of 0.01% for 1h, the activity of the enzyme at the control level was observed for all compounds, whereas at a concentration of 0.1% for 24 h, the activity increased sharply in the presence of compounds 1 (300%), 6 (153%), and 2 (134%). The action of the others was at the control level. Conclusions. The obtained data on new complex metal compounds with an activating effect on microbial α-L-rhamnosidases. It has been established that compounds whose structural organization ensures the synergism of the action of all components are the most promising enzyme effectors in a series of coordination compounds of biologically active metals and ligands.

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Section: ][Ge(hcit) 2 ]•3h 2 O (1); [Ni(phen) 3 ][Ge(hcit) 2 ]•2h 2 O...mentioning

confidence: 99%

Influence of New Types of Biscitratogermanates on Penicillium restrictum α-L-Rhamnosidase

et al. 2023

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“…[29][30][31][32]. α-L-Rhamnosidase activity was noted in most micromycetes with starch-degrading activity, especially in representatives of the genera Acremonium, Alternaria, Aspergillus, Cladosporium, Eurotium, Fusarium, Mortierella, Penicillium, Phoma, and Talaromyces [23,29,33]. Active producers are described among strains of P .…”

Section: Distribution Of α-L-rhamnosidases Among Microorganismsmentioning

confidence: 99%

MICROBIAL Α-L-Rhamnosidases: CLASSIFICATION, DISTRIBUTION, PROPERTIES AND PRACTICAL APPLICATION

Borzova

2023

Biotechnol. acta

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One of the important problems of current biotechnology is the usage of enzymes of microbial origin for destruction of poorly soluble compounds and synthesis of new drugs. In recent years a great deal of researchers’ attention has been given to such technologically promising carbohydrases as O-glycosylhydrolases catalyzing the hydrolysis of O-glycoside links in glycosides, oligo- and polysaccharides, glycolipids, and other glycoconjugates. Aim. The review provides data on the position of α-L-rhamnosidases in the modern hierarchical classification of glycosidases and presents data available in the literature on the features of the enzyme structure in various microorganisms. Methods. The publications from the following databases were analyzed: PubMed (https://pubmed.nsbi.nlm.nih.gov/), the Carbohydrate-Active enZYmes (http://www.cazy.org/), the BRENDA Enzyme Database (https://www.brenda-enzymes.org/). Results. Data on the physicochemical, catalytic, and kinetic properties of α-L-rhamnosidases in microorganisms of different taxonomic groups have been systematized. The peculiarities of the substrate specificity of the enzyme depending on the nature of the protein and the growing conditions of the producer are characterized. Conclusions. Functional properties and specificity action of microbial α-L-rhamnosidases suggest their broad-range applicability for food and animal feed processing, as well as obtaining biologically active compounds for the pharmaceutical industry and medicine.

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“…Fibrinolytic and fi brinogenolytic activities were determined by the recommended methods [13] with fi brin and fi brinogen as substrates.…”

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confidence: 99%

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2022

Mikrobiol. Z.

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Despite the fact that in recent years there has been a certain enhancing interest in the study of marine microorganisms, nevertheless, marine bacteria as producers of biologically active substances, in particular enzymes, are still poorly. studied. Th e marine biota is signifi cantly diff erent from the terrestrial one; therefore, there is a high probability of detecting in the marine environment diff erent from terrestrial bacteria producers of enzymes with unique specifi city and activity, for the needs of modern biotechnology. Proteolytic enzymes play an important role in these studies. Since the majority of microbial producers are characterized by a number of serious defi ciencies, in particular, most of the elastase producers described in the literature are pathogenic for humans, the search for new, eff ective producers continues to be an urgent problem, given that highly active producers of proteolytic enzymes, in particular elastase, are generally absent in Ukraine. In this regard, the purpose of this work was to screen microorganisms isolated from the Black Sea for the presence of eff ective producers of proteolytic enzymes. Methods. We used methods of determining proteolytic (caseinilytic, elastolytic, fi brinolytic, fi brinogenolytic) activity. Results. Th e study of the enzymatic activity of the isolates showed that on the 10th day of cultivation in the supernatant of the culture liquid, caseinolytic activity was not detected only in one isolate 56, whereas very insignifi cant activity was observed in isolates 7, 20, and 50. Th e maximum activity was detected in isolate 247 (0.2 units/mL), and lower one -in isolates 46 (0.16 U/mL), 52 (0.15 U/mL), 51 (0.135 U/mL), 54 (0.08 U/mL), and 44 (0.05 U/mL). Of the 10 studied isolates, elastase activity was found only in four of them. Th e highest activity was found in isolates 51 and 54 (20.83 and 19.96 U/mL, respectively). Lower levels of activity (15.62 U/mL and 12.15 U/mL, respectively) were shown by isolates 52 and 247. Th e studied isolates also diff ered in their ability to hydrolyze fi brin and fi brinogen. Th e highest fi brinolytic activity (2.33 U/mL) was found in isolates 46 and 54, signifi cantly lower in isolate 20 (0.5 U/mL) and isolate 44 (0.33 U/mL). Th e rest isolates did not show fi brinolytic activity. As for fi brinogenolytic activity, it was noted in 6 studied cultures. Th e highest levels of activity

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Thermophilic Fungi with Glucosidase and Proteolytic Activities

Cited by 4 publications

References 31 publications

Influence of New Types of Biscitratogermanates on Penicillium restrictum α-L-Rhamnosidase

Influence of New Types of Biscitratogermanates on Penicillium restrictum α-L-Rhamnosidase

MICROBIAL Α-L-Rhamnosidases: CLASSIFICATION, DISTRIBUTION, PROPERTIES AND PRACTICAL APPLICATION

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