Purification and Biochemical Characterization of a Novel Thermostable Serine Protease from Geobacillus sp. GS53

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dc.authorscopusid57221915111
dc.authorscopusid55758999000
dc.authorscopusid36680469600
dc.contributor.authorBaykara, S.G.
dc.contributor.authorSürmeli, Yusuf
dc.contributor.authorŞanlı Mohamed, Gülşah
dc.date.accessioned2022-05-11T14:07:12Z
dc.date.available2022-05-11T14:07:12Z
dc.date.issued2021
dc.departmentFakülteler, Ziraat Fakültesi, Tarımsal Biyoteknoloji Bölümü
dc.description.abstractProteases account for approximately 60% of the enzyme market in the world, and they are used in various industrial applications including the detergent industry. In this study, production and characterization of a novel serine protease of thermophilic Geobacillus sp. GS53 from Balçova geothermal region, İzmir, Turkey, were performed. The thermostable protease was purified through ammonium sulfate precipitation and anion-exchange chromatography. The results showed that the protease had 137.8 U mg?1 of specific activity and optimally worked at 55 oC and pH 8. It was also active in a broad pH (4–10) and temperature (25–75 °C) ranges. The protease was highly stable at 85 °C and demonstrated relative stability at pH 4, 7, and 10. Also, the enzyme had high stability against organic solvents and surfactants; enzyme relative activity did not decrease below 81% upon preincubation for 10 min. Ca2+, Cu2+, and Zn2+ ions slightly induced protease activity. The protease was highly specific to casein, skim milk, Hammerstein casein, and BSA substrates. These results revealed that the protease might have a potential effect in a variety of industrial fields, especially the detergent industry, because of its high thermostability and stability to surfactants. © 2021, The Author(s), under exclusive licence to Springer Science+Business Media, LLC part of Springer Nature.
dc.description.sponsorshipThe authors would like to thank Biotechnology & Bioengineering Research Center at ?zmir Institute of Technology for the facilities and technical support.
dc.identifier.doi10.1007/s12010-021-03512-0
dc.identifier.endpage1584
dc.identifier.issn0273-2289
dc.identifier.issue5en_US
dc.identifier.pmid33507494
dc.identifier.scopus2-s2.0-85100569779
dc.identifier.scopusqualityQ2
dc.identifier.startpage1574
dc.identifier.urihttps://doi.org/10.1007/s12010-021-03512-0
dc.identifier.urihttps://hdl.handle.net/20.500.11776/5007
dc.identifier.volume193
dc.identifier.wosWOS:000612570800002
dc.identifier.wosqualityQ3
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.institutionauthorSürmeli, Yusuf
dc.language.isoen
dc.publisherSpringer
dc.relation.ispartofApplied Biochemistry and Biotechnology
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectGeobacillus
dc.subjectSerine protease
dc.subjectSurfactant
dc.subjectThermostability
dc.subjectAmino acids
dc.subjectCasein
dc.subjectDairies
dc.subjectNitrogen compounds
dc.subjectPurification
dc.subjectSulfur compounds
dc.subjectSurface active agents
dc.subjectAmmonium sulfate precipitation
dc.subjectAnion exchange chromatography
dc.subjectBiochemical characterization
dc.subjectDetergent industry
dc.subjectIndustrial fields
dc.subjectProtease activities
dc.subjectRelative activities
dc.subjectRelative stabilities
dc.subjectEnzyme activity
dc.subjectalkaline proteinase
dc.subjectammonium sulfate
dc.subjectcalcium ion
dc.subjectcasein
dc.subjectcuprous ion
dc.subjectserine proteinase
dc.subjectzinc ion
dc.subjectcalcium
dc.subjectcopper
dc.subjectserine proteinase
dc.subjectsurfactant
dc.subjectzinc
dc.subjectanion exchange chromatography
dc.subjectArticle
dc.subjectbacterial strain
dc.subjectbiochemistry
dc.subjectcontrolled study
dc.subjectenzyme activity
dc.subjectenzyme purification
dc.subjectenzyme specificity
dc.subjectenzyme stability
dc.subjectGeobacillus
dc.subjectGeobacillus stearothermophilus
dc.subjectGeobacillus toebii
dc.subjection exchange chromatography
dc.subjectmolecular weight
dc.subjectnonhuman
dc.subjectpH
dc.subjectpolyacrylamide gel electrophoresis
dc.subjectprecipitation
dc.subjectskim milk
dc.subjecttemperature
dc.subjectTurkey (republic)
dc.subjectchemistry
dc.subjectenzyme stability
dc.subjectenzymology
dc.subjectGeobacillus
dc.subjectmetabolism
dc.subjectCalcium
dc.subjectChromatography, Ion Exchange
dc.subjectCopper
dc.subjectEnzyme Stability
dc.subjectGeobacillus
dc.subjectHydrogen-Ion Concentration
dc.subjectMolecular Weight
dc.subjectSerine Proteases
dc.subjectSubstrate Specificity
dc.subjectSurface-Active Agents
dc.subjectZinc
dc.titlePurification and Biochemical Characterization of a Novel Thermostable Serine Protease from Geobacillus sp. GS53
dc.typeArticle

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