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- Title
Enhancing stability and activity of β-galactosidase from Kluyveromyces lactis through immobilization on polymethacrylate monolith and optimisation using response surface methodology.
- Authors
Dahari, Rima Fatira; Misson, Mailin; Ongkudon, Clarence M; Saallah, Suryani; Asran, Aliyah Madihah; Dailin, Daniel Joe; Chuah, Lai Fatt; El Enshasy, Hesham
- Abstract
Aims: This study investigates the potential of porous polymethacrylate monoliths as enzyme support materials for largescale enzyme commercialization. Methodology and results: It focuses on their preparation and various immobilization techniques, such as adsorption, covalent-binding and cross-linking, specifically applied to β-galactosidase for bioprocess applications. The research assesses immobilization performance, operational stability, reusability and optimization using response surface methodology (RSM). The results reveal that covalent-binding exhibited the highest enzyme activity recovery, while cross-linking showed superior performance at lower enzyme concentrations but decreased at higher concentrations. Covalent-bound enzymes demonstrated reusability for up to four cycles, with optimal pH ranging between 7 and 8 and optimal temperature ranging between 30 °C and 40 °C. Furthermore, RSM optimization highlighted the significant influence of substrate concentration on enzyme activity, with a reliable model (R² = 0.9163) and adequate precision (S/N = 13.1409). Conclusion, significance and impact of study: Overall, this study provides valuable guidelines for effectively employing porous monoliths in large-scale industrial bioprocessing, offering potential cost-saving benefits and enhanced efficiency in enzyme commercialization.
- Subjects
GALACTOSIDASES; KLUYVEROMYCES marxianus; COMMERCIALIZATION; RESPONSE surfaces (Statistics); COST effectiveness
- Publication
Malaysian Journal of Microbiology, 2023, Vol 19, Issue 6, p752
- ISSN
1823-8262
- Publication type
Article
- DOI
10.21161/mjm.230023