Full metadata record
DC Field | Value | Language |
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dc.citation.endPage | 680 | - |
dc.citation.number | 9 | - |
dc.citation.startPage | 672 | - |
dc.citation.title | INDIAN JOURNAL OF EXPERIMENTAL BIOLOGY | - |
dc.citation.volume | 60 | - |
dc.contributor.author | Vishvakarma, Reena | - |
dc.contributor.author | Vimal, Archana | - |
dc.contributor.author | Mishra, Abha | - |
dc.contributor.author | Sharma, Poonam | - |
dc.contributor.author | Gaur, Vivek Kumar | - |
dc.date.accessioned | 2023-12-21T13:40:15Z | - |
dc.date.available | 2023-12-21T13:40:15Z | - |
dc.date.created | 2022-10-27 | - |
dc.date.issued | 2022-09 | - |
dc.description.abstract | 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.) Quel.; 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 & DEG;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 & DEG;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 & DEG;C) and pH (5.0-8.0) with a half-life of 58.72 min, Vmax of 37.17 mu M 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. | - |
dc.identifier.bibliographicCitation | INDIAN JOURNAL OF EXPERIMENTAL BIOLOGY, v.60, no.9, pp.672 - 680 | - |
dc.identifier.doi | 10.56042/ijeb.v60i09.65147 | - |
dc.identifier.issn | 0019-5189 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/60718 | - |
dc.identifier.wosid | 000862825700004 | - |
dc.language | 영어 | - |
dc.publisher | NATL INST SCIENCE COMMUNICATION-NISCAIR | - |
dc.title | Trametes versicolor (L.) Lloyd as a source of thermostable serine protease: production and characterization | - |
dc.type | Article | - |
dc.description.isOpenAccess | TRUE | - |
dc.relation.journalWebOfScienceCategory | Biology | - |
dc.relation.journalResearchArea | Life Sciences & Biomedicine - Other Topics | - |
dc.type.docType | Article | - |
dc.description.journalRegisteredClass | scie | - |
dc.subject.keywordAuthor | Basidiomycetes | - |
dc.subject.keywordAuthor | Central Composite Design (CCD) | - |
dc.subject.keywordAuthor | Coriolus versicolor | - |
dc.subject.keywordAuthor | Edible mushrooms | - |
dc.subject.keywordAuthor | Plackett-Burman Design (PBD) | - |
dc.subject.keywordAuthor | Polypore mushroom | - |
dc.subject.keywordAuthor | Polyporus versicolor | - |
dc.subject.keywordAuthor | Response Surface Methodology (RSM) | - |
dc.subject.keywordAuthor | Solid-state fermentation | - |
dc.subject.keywordAuthor | Trametes versicolor | - |
dc.subject.keywordAuthor | Turkey tail | - |
dc.subject.keywordPlus | ASPERGILLUS-NIGER | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.subject.keywordPlus | OPTIMIZATION | - |
dc.subject.keywordPlus | STRAINS | - |
dc.subject.keywordPlus | ACID PROTEASE | - |
dc.subject.keywordPlus | SOLID-STATE | - |
dc.subject.keywordPlus | EXTRACELLULAR PROTEASE | - |
dc.subject.keywordPlus | PROTEOLYTIC-ENZYMES | - |
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