Please use this identifier to cite or link to this item: http://nopr.niscpr.res.in/handle/123456789/60445

metadata.dc.identifier.doi: https://doi.org/10.56042/ijeb.v60i09.65147Title: Trametes versicolor (L.) Lloyd as a source of thermostable serine protease: production and characterizationAuthors: Vishvakarma, Reena
Vimal, Archana
Mishra, Abha
Sharma, Poonam
Gaur, Vivek KumarKeywords: Basidiomycetes;Central Composite Design (CCD);Coriolus versicolor;Edible mushrooms;Plackett-Burman Design (PBD);Polypore mushroom;Polyporus versicolor;Response Surface Methodology (RSM);Solid-state fermentation;Trametes versicolor;Trametes versicolor;Turkey tailIssue Date: Sep-2022Publisher: NIScPR-CSIR,IndiaAbstract: Proteases are ubiquitously present and are among the largest groups of commercially important enzymes. Here, we investigated a wood-rot basidiomycete Trametes versicolor (L.) Lloyd [Syn. Coriolus versicolor (L.) Quél.; Polyporus versicolor (L.) Fr.] as a source of the enzyme serine protease, its production, and optimized to obtain a higher yield of the enzyme.. The significant variables with optimized values for maximum production of the enzyme were temperature (30C), incubation time (120 h) and wheat bran (10 g). The yield increased by 30.76% by statistically optimizing the media. The optimized temperature and pH for the maximum protease activity was 50C and pH 7.0, respectively. The enzyme was purified through ion exchange (using DEAE cellulose 52 resin) and gel filtration chromatography (using Superdex 200 column). The purified enzyme had a retention time of 7 min in RP-HPLC. The enzyme was stable at a broad range of temperature (30-60C) and pH (5.0-8.0) with a half-life of 58.72 min, Vmax of 37.17 μM min/mL and Km of 0.657 mg/mL. Its activity was enhanced by Na+, Ca2+, Mg2+ ions and SDS surfactant. These properties make this enzyme a valuable candidate for industrial applications.Page(s): 672-680ISSN: 0975-1009 (Online); 0019-5189 (Print)Appears in Collections:IJEB Vol.60(09) [Sep 2022]

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