Enhanced enzymatic activity and stability by in situ entrapment of α-Glucosidase within super porous p(HEMA) cryogels during synthesis
Here, poly(2-hydroxyethyl methacrylate) (p(HEMA)) cryogel were prepared in the presence 0.48, 0.96, and 1.92 mL of α-Glucosidase enzyme (0.06 Units/mL) solutions to obtain enzyme entrapped superporous p(HEMA) cryogels, donated as α-Glucosidase@p(HEMA)-1, α-Glucosidase@p(HEMA)-2, and α-Glucosidase@p(...
| Main Authors: | , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2020-12-01
|
| Series: | Biotechnology Reports |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2215017X20305919 |
| _version_ | 1818597562627653632 |
|---|---|
| author | Sahin Demirci Mehtap Sahiner Selehattin Yilmaz Erdener Karadag Nurettin Sahiner |
| author_facet | Sahin Demirci Mehtap Sahiner Selehattin Yilmaz Erdener Karadag Nurettin Sahiner |
| author_sort | Sahin Demirci |
| collection | DOAJ |
| description | Here, poly(2-hydroxyethyl methacrylate) (p(HEMA)) cryogel were prepared in the presence 0.48, 0.96, and 1.92 mL of α-Glucosidase enzyme (0.06 Units/mL) solutions to obtain enzyme entrapped superporous p(HEMA) cryogels, donated as α-Glucosidase@p(HEMA)-1, α-Glucosidase@p(HEMA)-2, and α-Glucosidase@p(HEMA)-3, respectively. The enzyme entrapped p(HEMA) cryogels revealed no interruption for hemolysis and coagulation of blood rendering viable biomedical application in blood contacting applications. The α-Glucosidase@p(HEMA)-1 was found to preserve its’ activity% 92.3 ± 1.4 % and higher activity% against free α-Glucosidase enzymes in 15–60℃ temperature, and 4–9 pH range. The Km and Vmax values of α-Glucosidase@p(HEMA)-1 cryogel was calculated as 3.22 mM, and 0.0048 mM/min, respectively versus 1.97 mM, and 0.0032 mM/min, for free enzymes. The α-Glucosidase@p(HEMA)-1 cryogel was found to maintained enzymatic activity more than 50 % after 10 consecutive uses, and also preserved their activity more than 50 % after 10 days of storage at 25 ℃, whereas free α-Glucosidase enzyme maintained only 1.9 ± 0.9 % activity under the same conditions. |
| first_indexed | 2024-12-16T11:49:47Z |
| format | Article |
| id | doaj.art-26523bcabe244338990550d636b6a4d0 |
| institution | Directory Open Access Journal |
| issn | 2215-017X |
| language | English |
| last_indexed | 2024-12-16T11:49:47Z |
| publishDate | 2020-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Biotechnology Reports |
| spelling | doaj.art-26523bcabe244338990550d636b6a4d02022-12-21T22:32:45ZengElsevierBiotechnology Reports2215-017X2020-12-0128e00534Enhanced enzymatic activity and stability by in situ entrapment of α-Glucosidase within super porous p(HEMA) cryogels during synthesisSahin Demirci0Mehtap Sahiner1Selehattin Yilmaz2Erdener Karadag3Nurettin Sahiner4Department of Chemistry, Faculty of Sciences and Arts, Canakkale Onsekiz Mart University Terzioglu Campus, 17100, Canakkale, Turkey; Nanoscience and Technology Research and Application Center, Canakkale Onsekiz Mart University Terzioglu Campus, 17100, Canakkale, TurkeyDepartment of Fashion Design, Faculty of Canakkale Applied Science, Canakkale Onsekiz Mart University Terzioglu Campus, 17100, Canakkale, TurkeyDepartment of Chemistry, Faculty of Sciences and Arts, Canakkale Onsekiz Mart University Terzioglu Campus, 17100, Canakkale, TurkeyDepartment of Chemistry, Faculty of Sciences and Arts, Aydın Adnan Menderes University, 09010, Aydın, TurkeyDepartment of Chemistry, Faculty of Sciences and Arts, Canakkale Onsekiz Mart University Terzioglu Campus, 17100, Canakkale, Turkey; Nanoscience and Technology Research and Application Center, Canakkale Onsekiz Mart University Terzioglu Campus, 17100, Canakkale, Turkey; Department of Chemical and Biomolecular Engineering, University of South Florida, Tampa, FL, 33620 USA; Department of Ophthalmology, Morsani College of Medicine, University of South Florida, 12901 Bruce B Downs B. Downs Blv., MDC 21, Tampa, FL 33612, USA; Corresponding author at: Department of Chemistry, Faculty of Sciences and Arts, Canakkale Onsekiz Mart University Terzioglu Campus, 17100, Canakkale, Turkey.Here, poly(2-hydroxyethyl methacrylate) (p(HEMA)) cryogel were prepared in the presence 0.48, 0.96, and 1.92 mL of α-Glucosidase enzyme (0.06 Units/mL) solutions to obtain enzyme entrapped superporous p(HEMA) cryogels, donated as α-Glucosidase@p(HEMA)-1, α-Glucosidase@p(HEMA)-2, and α-Glucosidase@p(HEMA)-3, respectively. The enzyme entrapped p(HEMA) cryogels revealed no interruption for hemolysis and coagulation of blood rendering viable biomedical application in blood contacting applications. The α-Glucosidase@p(HEMA)-1 was found to preserve its’ activity% 92.3 ± 1.4 % and higher activity% against free α-Glucosidase enzymes in 15–60℃ temperature, and 4–9 pH range. The Km and Vmax values of α-Glucosidase@p(HEMA)-1 cryogel was calculated as 3.22 mM, and 0.0048 mM/min, respectively versus 1.97 mM, and 0.0032 mM/min, for free enzymes. The α-Glucosidase@p(HEMA)-1 cryogel was found to maintained enzymatic activity more than 50 % after 10 consecutive uses, and also preserved their activity more than 50 % after 10 days of storage at 25 ℃, whereas free α-Glucosidase enzyme maintained only 1.9 ± 0.9 % activity under the same conditions.http://www.sciencedirect.com/science/article/pii/S2215017X20305919EnzymeSuper porous cryogelEnzyme immobilization/entrapmentα-GlucosidaseEnzymatic reaction |
| spellingShingle | Sahin Demirci Mehtap Sahiner Selehattin Yilmaz Erdener Karadag Nurettin Sahiner Enhanced enzymatic activity and stability by in situ entrapment of α-Glucosidase within super porous p(HEMA) cryogels during synthesis Biotechnology Reports Enzyme Super porous cryogel Enzyme immobilization/entrapment α-Glucosidase Enzymatic reaction |
| title | Enhanced enzymatic activity and stability by in situ entrapment of α-Glucosidase within super porous p(HEMA) cryogels during synthesis |
| title_full | Enhanced enzymatic activity and stability by in situ entrapment of α-Glucosidase within super porous p(HEMA) cryogels during synthesis |
| title_fullStr | Enhanced enzymatic activity and stability by in situ entrapment of α-Glucosidase within super porous p(HEMA) cryogels during synthesis |
| title_full_unstemmed | Enhanced enzymatic activity and stability by in situ entrapment of α-Glucosidase within super porous p(HEMA) cryogels during synthesis |
| title_short | Enhanced enzymatic activity and stability by in situ entrapment of α-Glucosidase within super porous p(HEMA) cryogels during synthesis |
| title_sort | enhanced enzymatic activity and stability by in situ entrapment of α glucosidase within super porous p hema cryogels during synthesis |
| topic | Enzyme Super porous cryogel Enzyme immobilization/entrapment α-Glucosidase Enzymatic reaction |
| url | http://www.sciencedirect.com/science/article/pii/S2215017X20305919 |
| work_keys_str_mv | AT sahindemirci enhancedenzymaticactivityandstabilitybyinsituentrapmentofaglucosidasewithinsuperporousphemacryogelsduringsynthesis AT mehtapsahiner enhancedenzymaticactivityandstabilitybyinsituentrapmentofaglucosidasewithinsuperporousphemacryogelsduringsynthesis AT selehattinyilmaz enhancedenzymaticactivityandstabilitybyinsituentrapmentofaglucosidasewithinsuperporousphemacryogelsduringsynthesis AT erdenerkaradag enhancedenzymaticactivityandstabilitybyinsituentrapmentofaglucosidasewithinsuperporousphemacryogelsduringsynthesis AT nurettinsahiner enhancedenzymaticactivityandstabilitybyinsituentrapmentofaglucosidasewithinsuperporousphemacryogelsduringsynthesis |