Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/11422
Full metadata record
DC FieldValueLanguage
dc.contributor.authorGüracar Baykara, Sedentr
dc.contributor.authorSürmeli, Yusuftr
dc.contributor.authorŞanlı Mohamed, Gülşah-
dc.date.accessioned2021-11-06T09:48:31Z-
dc.date.available2021-11-06T09:48:31Z-
dc.date.issued2021-
dc.identifier.issn0273-2289-
dc.identifier.issn1559-0291-
dc.identifier.urihttps://doi.org/10.1007/s12010-021-03512-0-
dc.identifier.urihttps://hdl.handle.net/11147/11422-
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 Balcova geothermal region, Izmir, 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 C-o and pH 8. It was also active in a broad pH (4-10) and temperature (25-75 degrees C) ranges. The protease was highly stable at 85 degrees 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.en_US
dc.description.sponsorshipThe authors would like to thank Biotechnology & Bioengineering Research Center at Izmir Institute of Technology for the facilities and technical support.en_US
dc.language.isoenen_US
dc.publisherSpringeren_US
dc.relation.ispartofApplied Biochemistry and Biotechnologyen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectSerine proteaseen_US
dc.subjectGeobacillusen_US
dc.subjectThermostabilityen_US
dc.subjectSurfactanten_US
dc.titlePurification and biochemical characterization of a novel thermostable serine protease from Geobacillus sp. GS53en_US
dc.typeArticleen_US
dc.departmentİzmir Institute of Technology. Chemistryen_US
dc.identifier.volume193en_US
dc.identifier.issue5en_US
dc.identifier.startpage1574en_US
dc.identifier.endpage1584en_US
dc.identifier.wosWOS:000612570800002en_US
dc.identifier.scopus2-s2.0-85100569779en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıtr
dc.identifier.doi10.1007/s12010-021-03512-0-
dc.identifier.pmid33507494en_US
dc.identifier.wosqualityQ3-
dc.identifier.scopusqualityQ2-
item.openairetypeArticle-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextWith Fulltext-
item.languageiso639-1en-
item.cerifentitytypePublications-
item.grantfulltextopen-
crisitem.author.dept04.01. Department of Chemistry-
Appears in Collections:Chemistry / Kimya
PubMed İndeksli Yayınlar Koleksiyonu / PubMed Indexed Publications Collection
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection
Files in This Item:
File SizeFormat 
s12010-021-03512-0.pdf621.48 kBAdobe PDFView/Open
Show simple item record



CORE Recommender

SCOPUSTM   
Citations

7
checked on Mar 22, 2024

WEB OF SCIENCETM
Citations

4
checked on Mar 23, 2024

Page view(s)

760
checked on Mar 25, 2024

Download(s)

64
checked on Mar 25, 2024

Google ScholarTM

Check




Altmetric


Items in GCRIS Repository are protected by copyright, with all rights reserved, unless otherwise indicated.