Cloning, expression and characterization of bacterial L-arabinose isomerase / Hoda Mohamed Shehata Ahmed ; Supervised Zeinat Kamel Mohamed Ibrahim , Mohamed Gamal Salah Farahat , Mohamed Eweis Mahmoud Ahmed
Material type: TextLanguage: English Publication details: Cairo : Hoda Mohamed Shehata Ahmed , 2021Description: 112 P . : charts ; 25cmOther title:- إستنساخ وتعبير وتوصيف ل-ارابينوز ايزوميريز البكتيرى [Added title page title]
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Item type | Current library | Home library | Call number | Copy number | Status | Date due | Barcode | |
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Thesis | قاعة الرسائل الجامعية - الدور الاول | المكتبة المركزبة الجديدة - جامعة القاهرة | Cai01.12.05.Ph.D.2021.Ho.C (Browse shelf(Opens below)) | Not for loan | 01010110083369000 | |||
CD - Rom | مخـــزن الرســائل الجـــامعية - البدروم | المكتبة المركزبة الجديدة - جامعة القاهرة | Cai01.12.05.Ph.D.2021.Ho.C (Browse shelf(Opens below)) | 83369.CD | Not for loan | 01020110083369000 |
Thesis (Ph.D.) - Cairo University - Faculty of Science - Department of Botany and Microbiology
L-Arabinose isomerase genes from Bacillus amyloliquefaciens CAAI and Enterococcus faecium SCAI were cloned and over-expressed in Escherichia coli as soluble and functional proteins. The recombinant enzymes were purified to apparent homogeneity by Ni-NTA affinity chromatography and partially characterized. Besides, biosynthesis of D-tagatose was achieved by constructing and expressing a polycistronic plasmid encoding codon-optimized thermostable Ý-galactosidase from Marinomonas sp. BSi20414 and L-arabinose isomerase from Clostridium hylemonae, simultaneously, in Lactococcus lactis NZ3900. Results revealed an efficient bioconversion of lactose to D-tagatose and maximum production was accomplished at 60{u00B0}C after 12 h, starting with 20% (w/v) lactose. The induced recombinant cells entrapped in chitosan beads converted up to 34% of lactose into D-tagatose in a single step that could be implemented in safe-production of food-grade low-calorie sweetener
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