β-Mannanase Activity of Yeasts Isolated in Antarctic

Borzova, N.V.; Gladka, Galina; Varbanets, L.D.; Tashyrev, Oleksandr

doi:10.15407/microbiolj80.02.028

Cited by 4 publications

(2 citation statements)

References 19 publications

(27 reference statements)

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“…Additionally, enzymes obtained from cold places such as the Antarctic pole can also present activity at extreme low temperatures [10]. Th erefore, these enzymes might remain active under varied operational conditions, providing competitiveness and effi ciency to diff erent industrial processes [11].…”

Section: Methodsmentioning

confidence: 99%

Untitled

2023

Mikrobiol. Z.

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For a long time, the main interest in the marine environment, considered extreme, was the isolation and identifi cation of natural products with biological properties, and for that, numerous organisms and chemical structures have been studied. Th us, marine bacteria isolated from various substrates, such as sediments, seawater, and mangrove detritus, are producers of enzymes with diff erent activities, i.e., amylase, cellulase, alginate lyase, chitinase, glucosidase, inulinase, keratinase, ligninase, xylanase, and others. Nowadays, researchers are also focusing on the enzymes produced in the marine environment that can present special properties. Th erefore, the aim of this study was to investigate the ability of marine strains of microorganisms to exhibit cellulase, β-mannanase, keratinase, and caseinolytic activities. Methods. Enzymatic activities were studied in the culture liquid supernatant. To determine β-mannanase and cellulase activities, guar gum galactomannan and Na-carboxymethylcellulose respectively were used as substrates. Casein and crushed defatted feathers served as substrates for the determination of proteolytic activity. Results. Growing 10 cultures of microorganisms on a nutrient medium containing chicken feathers as the sole source of carbon and nitrogen (nutrient medium 1) did not give positive results. When using medium 2, active growth was observed in four of the studied strains (51, 52, 54, 247) in the supernatant of culture liquid (CLS), the activity of which both to keratin (6.0-16.0 U/mL) and casein (0.025-0.33 U/mL) was found. In the CLS of only six of the 10 studied cultures (7, 20, 51, 52, 50, 247), cellulase and β-mannanase activities were observed. Th e highest cellulase activity was found in culture 20 (1.8 U/mL). Th e activity of culture 7 was somewhat lower (1.0 U/mL). An insignifi cant activity was noted in cultures 54 (0.06 U/mL), 56, and 50 (0.05 U/mL). Trace levels of activity were observed in culture 247. Conclusions. Strains 7, 20, 247, and 51, for the fi rst time isolated from the Black Sea, are promising for further studies as producers of cellulase, β-mannanase, keratinase, and caseinolytic enzymes.

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Section: Methodsmentioning

confidence: 99%

Untitled

2023

Mikrobiol. Z.

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“…Раніше нами вже відмічалася індукція синтезу глікозидаз у присутності рамнози, яка мала як специфічний, так і неспецифічний характер. Так, індукція синтезу нарингінази може бути пояснена специфічністю до субстрату [16], а підвищення виходу манан-деградувальних ензимів дріжджів при культивуванні на середовищі з рамнозою пов'язано з іншим фізіологіч-ним механізмом і особливостями метаболізму продуцентів [17].…”

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Features of α-Galactosidase Production by Penicillium restrictum

Borzova¹,

Гудзенко²,

Varbanets³

2020

Mikrobiol. Z.

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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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β-Mannanase Activity of Yeasts Isolated in Antarctic

Cited by 4 publications

References 19 publications

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Features of α-Galactosidase Production by Penicillium restrictum

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

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