METALLOPROTEASE FROM THE CULTURAL LIQUID OF Pleurotus osreatus

Sakovich, V. V.; Ye., M Stohnii; Zhernosekov, D. D.; Rebriev, A. V.; Korolova, Daria; Yu., Marunych R.; Chernyshenko, Volodymyr

doi:10.15407/biotech12.06.035

Cited by 4 publications

(7 citation statements)

References 17 publications

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“…Temperature. The activity of the enzyme preparation from P.ostreatus culture fluid was observed in the temperature range from 25 to 60 ° C. In this case, the temperature optimum of proteolytic activity is at 45 ° C [41,42].…”

Section: Aspartic Proteinases From Basidiomycetesmentioning

confidence: 99%

“…A high degree of hydrolysis of the Leu-pNa substrate can be explained by the fact that both amino acids (Leu and Phe) according to the modern classification belong to the same group (amino acids containing non-polar hydrophobic R-groups). The authors recommend Leu-pNa for the work with the enzyme preparation from the culture fluid [42].…”

Section: Aspartic Proteinases From Basidiomycetesmentioning

confidence: 99%

“…The molecular weight of the aspartic enzyme obtained from the culture fluid of P.ostreatus is 45 kDa. So, proteases from fruiting bodies and culture fluid are similar in molecular weight [37,39,42].…”

Section: Molecular Massmentioning

confidence: 99%

“…The preparation of milk-clotting enzyme was obtained from the culture fluid, which has a more significant milk-clotting activity than the enzymes obtained from fruiting bodies. Isolation, purification and study of the properties of these enzymes are a necessary vector for modern biotechnology [41,42].…”

Section: Prospects For the Use Of Aspartate Proteinasesmentioning

confidence: 99%

“…One of the promising sources for obtaining fibrinolytic enzymes is the enzymes from the common P.ostreatus. There are some reports about isolation and purification of fibrinolytic proteinases from fruiting bodies [37,38], as well as from the culture fluid of P.ostreatus [42]. Recently it has been shown that proteinase from the culture fluid of oyster mushroom ordinary selectively degrades the Aa chain of fibrinogen, cleaving first the polypeptide with a molecular mass of approximately 3 kDa, and then another portion with a molecular weight of 10-15 kDa.…”

Section: Fibrinolytic Properties Of Fungal Proteasesmentioning

confidence: 99%

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Structural and functional peculiarities of aspartic proteases of basidiomycetes

Sakovich

2020

Biopolym. Cell

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The vast diversity of fungal proteases and the specificity of their action have attracted attention in attempts to exploit their physiological and biotechnological applications. These enzymes are widely used in biotechnology, mainly in food, leather, and detergent industries, in ecological bioremediation processes and to produce therapeutic peptides. This review covers various aspects of aspartic proteases from basidiomycetes including sources, production, structural peculiarities, physicochemical properties and their diverse applications. K e y w o r d s: Proteolytic enzymes, physical and chemical properties

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Section: Aspartic Proteinases From Basidiomycetesmentioning

confidence: 99%

Section: Aspartic Proteinases From Basidiomycetesmentioning

confidence: 99%

Section: Molecular Massmentioning

confidence: 99%

Section: Prospects For the Use Of Aspartate Proteinasesmentioning

confidence: 99%

Section: Fibrinolytic Properties Of Fungal Proteasesmentioning

confidence: 99%

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Structural and functional peculiarities of aspartic proteases of basidiomycetes

Sakovich

2020

Biopolym. Cell

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Edible Mushrooms as Source of Fibrin(ogen)olytic Enzymes: Comparison between Four Cultivated Species

et al. 2022

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Cardiovascular diseases represent the main cause of death. A common feature of cardiovascular disease is thrombosis resulting from intravascular accumulation of fibrin. In the last years, several fibrinolytic enzymes have been discovered in many medicinal or edible mushrooms as potential new antithrombotic agents. This study aimed to compare the fibrin(ogen)olytic activity of crude extracts from the fruiting bodies of four cultivated edible mushrooms: Lentinula edodes, Pleurotus ostreatus, Pleurotus eryngii, and Agrocybe aegerita. Fibrin(ogen)olytic activity was assessed by fibrin plate, spectrophotometric assay and electrophoretic analysis (SDS-PAGE and zymography). The highest activity was detected for P. ostreatus followed by P. eryngii, L. edodes and A. aegerita. Results indicated that enzymes exhibited maximum activity at pH 6–7 and 30–40 °C, respectively. Enzyme activity was inhibited by serine and metalloprotease inhibitors. We proposed a new index called the Specific Fibrin(ogen)olytic Index (SFI), which allows specification of the proportion of the total proteolytic capacity due to the fibrin(ogen)olytic activity. These data suggest that the extracts from fruiting bodies or powdered mushrooms can be used as functional ingredients for the development of new functional foods that may act as thrombolytic agents responding, at the same time, to the increasing demand for safe, healthy and sustainable food.

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Fibrin(ogen)olytic and platelet modulating properties of a novel protease from the culture fluid of Pleurotus osreatus

et al. 2020

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The use of proteases makes it possible to obtain partially hydrolyzed forms of macromolecules with unique properties. The importance of proteases for studying the structure and functions of fibrinogen forces scientists to search for new sources of highly specific proteases. Thus, the aim of this work was to study the content of the Pleurotus ostreatus culture fluid in search of fibrinogen-specific proteases. P. ostreatus was cultured for 14 days at 27 ° C. The culture fluid was collected and the protein fraction was salted out with NaCl and then dialyzed. Fibrinogen hydrolysis products by P. ostreatus protease were characterized using SDS PAGE under reducing conditions followed by immunoprobing using murine monoclonal antibodies I-5A (anti-Aα505-610) and 2d2a (anti-Bβ26-42). The study of turbidity and platelet aggregation was performed using a Multiskan FC spectrophotometric microplate reader and a SOLAR-2110 aggregometer, respectively. Electron microscopy of fibrils formed by truncated compared with native fibrins was performed using a transmission electron microscope N-600.Analysis of the products of fibrinogen hydrolysis with a fungal protease using SDS-PAGE demonstrated the cleavage of the alpha chain of fibrinogen exclusively with the formation of a truncated form of fibrinogen in which there are no C-terminal portions of αC regions with a molecular weight of 25 kDa. A study of turbidity showed that the polymerization of truncated fibrin is significantly impaired. The rate of lateral association of protofibrils significantly decreased from 1.5 to 2.2 times in the case of truncated fibrinogen compared to the native one depending on the initial concentration of fibrinogen. It was shown that platelet aggregation in the presence of fibrinogen without 25 kDa fragments of αC regions was less effective than in the presence of native fibrinogen. Application of the preparation of the fungal protease allows us to obtain high molecular forms of the fibrinogen molecule with cleaved 25 kDa peptides, which provide new information on the role of these peptides in the fibrinogen functioning.

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METALLOPROTEASE FROM THE CULTURAL LIQUID OF Pleurotus osreatus

Cited by 4 publications

References 17 publications

Structural and functional peculiarities of aspartic proteases of basidiomycetes

Structural and functional peculiarities of aspartic proteases of basidiomycetes

Edible Mushrooms as Source of Fibrin(ogen)olytic Enzymes: Comparison between Four Cultivated Species

Fibrin(ogen)olytic and platelet modulating properties of a novel protease from the culture fluid of Pleurotus osreatus

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