Immobilization of maltase from Saccharomyces cerevisiae on thiosulfonate supports
| العنوان: | Immobilization of maltase from Saccharomyces cerevisiae on thiosulfonate supports |
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| المؤلفون: | Milica Carević, Katarina Banjanac, Dušan Veličković, Mladen Mihailović, Jovana Trbojevic-Ivic, Dejan Bezbradica, Nenad Milosavić |
| المصدر: | Journal of the Serbian Chemical Society Journal of the Serbian Chemical Society, Vol 81, Iss 12, Pp 1371-1382 (2016) |
| بيانات النشر: | National Library of Serbia, 2016. |
| سنة النشر: | 2016 |
| مصطلحات موضوعية: | 0106 biological sciences, 0301 basic medicine, Saccharomyces cerevisiae, 01 natural sciences, lcsh:Chemistry, 03 medical and health sciences, Adsorption, 010608 biotechnology, Organic chemistry, Eupergit® C, alpha-glucosidase, Purolite® A109, chemistry.chemical_classification, Purolite (R) A109, covalent disulfide bridges, biology, General Chemistry, biology.organism_classification, Combinatorial chemistry, 030104 developmental biology, Enzyme, lcsh:QD1-999, chemistry, Covalent bond, Reagent, Thiol, α-glucosidase, Maltase, Eupergit (R) C, Cysteine |
| الوصف: | In this study, two commercial supports (Eupergit® C and Purolite® A109) were chemically modified in order to introduce thiosulfonate groups, which could subsequently exclusively react with cysteine residues on enzyme surface. Thereafter, the immobilization of maltase from Saccharomyces cerevisiae onto obtained thiosulfonate-activated supports was performed, resulting in high expressed enzymatic activities (around 50%), while on the other hand, immobilization on unmodified supports yielded expressed activities less than 5%. Moreover, protein loadings up to 12.3 mg g-1 and immobilized activities up to 3580 IU g-1 were achieved by employment of theses thiosulfonate supports. Desorption experiments, performed on samples taken during immobilization, proved that immobilization on thiosulfonate supports encompass first step of fast adsorption on support and second slower step of the covalent bond formation between thiosulfonate groups and thiol groups of cysteine. More importantly, although enzyme coupling occurs via covalent bond formation, performed immobilization proved to be reversible, since it was shown that 95% of immobilized activity can be detached from support after treatment with thiol reagent (β-mercaptoethanol), thus support can be reused after enzyme inactivation. [Projekat Ministarstva nauke Republike Srbije, br. III 46010] |
| تدمد: | 1820-7421 0352-5139 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5bf47b78b24ed5886b90955ca457c52 https://doi.org/10.2298/jsc160730099m |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....e5bf47b78b24ed5886b90955ca457c52 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 18207421 03525139 |
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