Immobilization of B. amyloliquefaciens ?-amylase and comparison of some of its enzymatic properties with the free form
dc.authorid | Ertan, Figen/0000-0002-7882-3993 | |
dc.authorwosid | Demirkan, Elif/ABI-4472-2020 | |
dc.contributor.author | Demirkan, Elif | |
dc.contributor.author | Dincbas, Serhan | |
dc.contributor.author | Sevinc, Nihan | |
dc.contributor.author | Ertan, Figen | |
dc.date.accessioned | 2024-06-12T10:51:19Z | |
dc.date.available | 2024-06-12T10:51:19Z | |
dc.date.issued | 2011 | |
dc.department | Trakya Üniversitesi | en_US |
dc.description.abstract | The enzyme alpha-Amylase from Bacillus amyloliquefaciens was entrapped by drop-wise addition of an aqueous mixture of sodium alginate in the solution of a Ca2+ salt. Effects of immobilization conditions were investigated. Optimum alginate and CaCl2 concentrations were found to be 2% and 5% (w/v), respectively. The immobilization yield was 89%. Amylase activity increased with increasing enzyme loading on the beads. The best size and amount of beads for achieving enzyme activity were found to be 3 mm and 0.4 g, respectively. When coated with silicate, amylase-entrapped beads retained the highest catalytic activity. The highest operational stability was six reuses with 51% residual activity. Some properties of immobilized enzyme were determined, and compared with those of free enzyme. Product profile of the various raw starches has been determined by thin layer chromatography. | en_US |
dc.description.sponsorship | Uludag University Commission of Scientific Research [F-2008/24] | en_US |
dc.description.sponsorship | This research was funded by Uludag University Commission of Scientific Research Projects, Grant F-2008/24, which is highly appreciated. | en_US |
dc.identifier.endpage | 6701 | en_US |
dc.identifier.issn | 1224-5984 | |
dc.identifier.issue | 6 | en_US |
dc.identifier.scopus | 2-s2.0-84858328042 | en_US |
dc.identifier.scopusquality | N/A | en_US |
dc.identifier.startpage | 6690 | en_US |
dc.identifier.uri | https://hdl.handle.net/20.500.14551/18312 | |
dc.identifier.volume | 16 | en_US |
dc.identifier.wos | WOS:000299089600003 | en_US |
dc.identifier.wosquality | Q4 | en_US |
dc.indekslendigikaynak | Web of Science | en_US |
dc.indekslendigikaynak | Scopus | en_US |
dc.language.iso | en | en_US |
dc.publisher | Ars Docendi | en_US |
dc.relation.ispartof | Romanian Biotechnological Letters | en_US |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |
dc.rights | info:eu-repo/semantics/closedAccess | en_US |
dc.subject | Alpha-Amylase | en_US |
dc.subject | Bacillus Amyloliquefaciens | en_US |
dc.subject | Calcium Alginate | en_US |
dc.subject | Immobilization | en_US |
dc.subject | Optimization | en_US |
dc.subject | Thin Layer Chromatography | en_US |
dc.subject | Alginate Beads | en_US |
dc.subject | Starch | en_US |
dc.subject | Hydrolysis | en_US |
dc.subject | Lipase | en_US |
dc.subject | Optimization | en_US |
dc.subject | Purification | en_US |
dc.subject | Entrapment | en_US |
dc.subject | Stability | en_US |
dc.subject | Matrix | en_US |
dc.title | Immobilization of B. amyloliquefaciens ?-amylase and comparison of some of its enzymatic properties with the free form | en_US |
dc.type | Article | en_US |