Immobilization of hyperthermostable carboxylesterase EstD9 from Anoxybacillus geothermalis D9 onto Polymer material and its physicochemical properties
Carboxylesterase has much to offer in the context of environmentally friendly and sustainable alternatives. However, due to the unstable properties of the enzyme in its free state, its application is severely limited. The present study aimed to immobilize hyperthermostable carboxylesterase from Anox...
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| Format: | Article |
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Multidisciplinary Digital Publishing Institute
2023
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| author | Mohd. Johan, Ummie Umaiera Raja Abd. Rahman, Raja Noor Zaliha Ahmad Kamarudin, Nor Hafizah Latip, Wahhida Mohamad Ali, Mohd Shukuri |
| author_facet | Mohd. Johan, Ummie Umaiera Raja Abd. Rahman, Raja Noor Zaliha Ahmad Kamarudin, Nor Hafizah Latip, Wahhida Mohamad Ali, Mohd Shukuri |
| author_sort | Mohd. Johan, Ummie Umaiera |
| collection | UPM |
| description | Carboxylesterase has much to offer in the context of environmentally friendly and sustainable alternatives. However, due to the unstable properties of the enzyme in its free state, its application is severely limited. The present study aimed to immobilize hyperthermostable carboxylesterase from Anoxybacillus geothermalis D9 with improved stability and reusability. In this study, Seplite LX120 was chosen as the matrix for immobilizing EstD9 by adsorption. Fourier-transform infrared (FT-IR) spectroscopy verified the binding of EstD9 to the support. According to SEM imaging, the support surface was densely covered with the enzyme, indicating successful enzyme immobilization. BET analysis of the adsorption isotherm revealed reduction of the total surface area and pore volume of the Seplite LX120 after immobilization. The immobilized EstD9 showed broad thermal stability (10–100 °C) and pH tolerance (pH 6–9), with optimal temperature and pH of 80 °C and pH 7, respectively. Additionally, the immobilized EstD9 demonstrated improved stability towards a variety of 25% (v/v) organic solvents, with acetonitrile exhibiting the highest relative activity (281.04%). The bound enzyme exhibited better storage stability than the free enzyme, with more than 70% of residual activity being maintained over 11 weeks. Through immobilization, EstD9 can be reused for up to seven cycles. This study demonstrates the improvement of the operational stability and properties of the immobilized enzyme for better practical applications. |
| first_indexed | 2024-09-25T03:40:52Z |
| format | Article |
| id | upm.eprints-108266 |
| institution | Universiti Putra Malaysia |
| last_indexed | 2024-09-25T03:40:52Z |
| publishDate | 2023 |
| publisher | Multidisciplinary Digital Publishing Institute |
| record_format | dspace |
| spelling | upm.eprints-1082662024-09-10T07:50:46Z http://psasir.upm.edu.my/id/eprint/108266/ Immobilization of hyperthermostable carboxylesterase EstD9 from Anoxybacillus geothermalis D9 onto Polymer material and its physicochemical properties Mohd. Johan, Ummie Umaiera Raja Abd. Rahman, Raja Noor Zaliha Ahmad Kamarudin, Nor Hafizah Latip, Wahhida Mohamad Ali, Mohd Shukuri Carboxylesterase has much to offer in the context of environmentally friendly and sustainable alternatives. However, due to the unstable properties of the enzyme in its free state, its application is severely limited. The present study aimed to immobilize hyperthermostable carboxylesterase from Anoxybacillus geothermalis D9 with improved stability and reusability. In this study, Seplite LX120 was chosen as the matrix for immobilizing EstD9 by adsorption. Fourier-transform infrared (FT-IR) spectroscopy verified the binding of EstD9 to the support. According to SEM imaging, the support surface was densely covered with the enzyme, indicating successful enzyme immobilization. BET analysis of the adsorption isotherm revealed reduction of the total surface area and pore volume of the Seplite LX120 after immobilization. The immobilized EstD9 showed broad thermal stability (10–100 °C) and pH tolerance (pH 6–9), with optimal temperature and pH of 80 °C and pH 7, respectively. Additionally, the immobilized EstD9 demonstrated improved stability towards a variety of 25% (v/v) organic solvents, with acetonitrile exhibiting the highest relative activity (281.04%). The bound enzyme exhibited better storage stability than the free enzyme, with more than 70% of residual activity being maintained over 11 weeks. Through immobilization, EstD9 can be reused for up to seven cycles. This study demonstrates the improvement of the operational stability and properties of the immobilized enzyme for better practical applications. Multidisciplinary Digital Publishing Institute 2023 Article PeerReviewed Mohd. Johan, Ummie Umaiera and Raja Abd. Rahman, Raja Noor Zaliha and Ahmad Kamarudin, Nor Hafizah and Latip, Wahhida and Mohamad Ali, Mohd Shukuri (2023) Immobilization of hyperthermostable carboxylesterase EstD9 from Anoxybacillus geothermalis D9 onto Polymer material and its physicochemical properties. Polymers, 15 (6). art. no. 1361. pp. 1-18. ISSN 2073-4360 https://www.mdpi.com/2073-4360/15/6/1361 10.3390/polym15061361 |
| spellingShingle | Mohd. Johan, Ummie Umaiera Raja Abd. Rahman, Raja Noor Zaliha Ahmad Kamarudin, Nor Hafizah Latip, Wahhida Mohamad Ali, Mohd Shukuri Immobilization of hyperthermostable carboxylesterase EstD9 from Anoxybacillus geothermalis D9 onto Polymer material and its physicochemical properties |
| title | Immobilization of hyperthermostable carboxylesterase EstD9 from Anoxybacillus geothermalis D9 onto Polymer material and its physicochemical properties |
| title_full | Immobilization of hyperthermostable carboxylesterase EstD9 from Anoxybacillus geothermalis D9 onto Polymer material and its physicochemical properties |
| title_fullStr | Immobilization of hyperthermostable carboxylesterase EstD9 from Anoxybacillus geothermalis D9 onto Polymer material and its physicochemical properties |
| title_full_unstemmed | Immobilization of hyperthermostable carboxylesterase EstD9 from Anoxybacillus geothermalis D9 onto Polymer material and its physicochemical properties |
| title_short | Immobilization of hyperthermostable carboxylesterase EstD9 from Anoxybacillus geothermalis D9 onto Polymer material and its physicochemical properties |
| title_sort | immobilization of hyperthermostable carboxylesterase estd9 from anoxybacillus geothermalis d9 onto polymer material and its physicochemical properties |
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