Characterization of a novel lipase bound to the Geobacillus stearothermophilus AH22 membrane

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dc.authorid0000-0001-8848-6647
dc.authorid0000-0001-9591-5411
dc.contributor.authorDincer, Barbaros
dc.contributor.authorIskender, Engin
dc.contributor.authorKizil, Demet
dc.contributor.authorAdiguzel, Ahmet
dc.date.accessioned2026-02-08T15:15:03Z
dc.date.available2026-02-08T15:15:03Z
dc.date.issued2025
dc.departmentBursa Teknik Üniversitesi
dc.description.abstractLipases (EC 3.1.1.3), used in many industrial applications, hydrolyze tri-, di-, and monoglycerides to free fatty acids and glycerol. This study aimed to determine the capacity of Geobacillus stearothermophilus AH22 for membrane-bound lipase production and to identify the optimal medium for lipase production. Following the determination of certain parameters such as pH and temperature, where the produced membrane-bound lipase exhibits the best activity, the kinetic data, as Km and Vmax, were obtained in the presence of p-NPA (0.03 +/- 0.008 mM and 0.7 +/- 0.18 U), p-NPB (0.7 +/- 0.18 mM and 3.4 +/- 0.40 U), p-NPO (0.12 +/- 0.010 mM and 5.2 +/- 0.62 U), and p-NPL (0.01 +/- 0.003 mM and 0.8 +/- 0.15 U) substrates. The highest activity of AH22 membrane-bound lipase was observed at pH 9.0 in the presence of substrates, at temperatures ranging from 20 to 40 degrees C for substrates with low carbon chains fatty acids and from 50 to 60 degrees C for substrates with long carbon chains. Also, it was observed that the cells dried by lyophilization showed lipase activity after they were pulver-ized. However, in terms of reuse, it was determined that wet cells were more efficient than powdered cells. It was found that the activity of the AH22 membrane-bound lipase had not changed much in the presence of anions and cations but decreased significantly in the presence of detergents and beta-mercaptoethanol. The AH22 membrane-bound lipase can be directly used in other industrial areas where lipase is used, except for the detergent industry, without requiring additional and expensive processing such as purification or immobilization.
dc.identifier.doi10.1007/s13205-025-04584-z
dc.identifier.issn2190-572X
dc.identifier.issn2190-5738
dc.identifier.issue12
dc.identifier.pmid41280477
dc.identifier.scopus2-s2.0-105022605272
dc.identifier.scopusqualityQ1
dc.identifier.urihttps://doi.org/10.1007/s13205-025-04584-z
dc.identifier.urihttps://hdl.handle.net/20.500.12885/5574
dc.identifier.volume15
dc.identifier.wosWOS:001620508700001
dc.identifier.wosqualityQ2
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherSpringer Heidelberg
dc.relation.ispartof3 Biotech
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/openAccess
dc.snmzWOS_KA_20260207
dc.subjectGeobacillus stearothermophilus
dc.subjectThermophilic bacteria
dc.subjectMembrane-bound lipase
dc.subjectIndustrial enzymes
dc.titleCharacterization of a novel lipase bound to the Geobacillus stearothermophilus AH22 membrane
dc.typeArticle

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