Enhancing stability and activity of β-galactosidase from Kluyveromyces lactis  through immobilization on polymethacrylate monolith and optimisation using response surface methodology

Rima Fatira Dahari; Mailin Misson; Clarence M Ongkudon; Suryani Saallah; Aliyah Madihah Asran; Daniel Joe Dailin; Lai Fatt Chuah; Hesham El Enshasy

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Enhancing stability and activity of β-galactosidase from Kluyveromyces lactis through immobilization on polymethacrylate monolith and optimisation using response surface methodology

Author: Rima Fatira Dahari ¹ ; Mailin Misson ¹ ; Clarence M Ongkudon ¹ ; Suryani Saallah ¹ ; Aliyah Madihah Asran ¹ ; Daniel Joe Dailin ^{2
,

3} ; Lai Fatt Chuah ⁴ ; Hesham El Enshasy ^{2
,

3
,

5}
Author Information

1. Biotechnology Research Institute, Universiti Malaysia Sabah, Jalan UMS, 88400 Kota Kinabalu, Sabah, Malaysia.
2. Institute of Bioproduct Development, Universiti Teknologi Malaysia, 81310, Skudai, Johor, Malaysia.&
3. Department of Biopress and Polymer Engineering, Faculty of Chemical and Energy Engineering, Universiti Teknologi Malaysia, 81310, Skudai, Johor, Malaysia.&
4. Faculty of Maritime Studies, Universiti Malaysia Terengganu, Terengganu, Malaysia.
5. Bioprocess Development Department, City for Scientific Research and Technology Applications (SRTA), New Burg Al Arab, Alexandria, Egypt.
Publication Type:Journal Article
Keywords: β-galactosidase; immobilization; polymethacrylate monolith; reusability; stability
From:Malaysian Journal of Microbiology 2023;19(no.6):752-765
CountryMalaysia
Language:English
Abstract: Aims:This study investigates the potential of porous polymethacrylate monoliths as enzyme support materials for large-scale 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.
Full text:20.2023my0079.pdf