Malaysian Journal of Biochemistry
& Molecular Biology
(E-ISSN: 2600-9005)
The Official Publication of the Malaysian Society for Biochemistry & Molecular Biology (MSBMB)
Indexed by SCOPUS and Malaysian Citation Index (MYCITE)
NEW ANNOUNCEMENT
The MJBMB will be revising its publication fee for accepted papers from MYR250 to MYR300 effective 1st January 2026.
New submissions received from 1st January 2026 onwards will pay the new rate.
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Special Issue (1) 2026
Selected Papers from the:
Korea-Asean Joint Symposium on Biomass Utilisation and Renewable Energy 2024 & AFOB Regional Symposium 2025
Page range 1-67
DOI:
Page 30-38
Chan Hui Min, Siti Fatimah Zaharah Mohd Fuzi, Aizi Nor Mazila Ramli, Apriliana Cahya Khayrani, Rosli Md. Illias and Nor Hasmaliana Abdul Manas
OPTIMIZED ENCAPSULATION OF MALTOGENIC AMYLASE IN CHITOSAN-COATED ALGINATE BEADS FOR ENHANCED ACTIVITY
Abstract
Oligosaccharides with non-digestible properties have attracted global attention due to their functional applications in the food and pharmaceutical industries. Malto-oligosaccharides, valued for their reducing properties, can be enzymatically produced from starch using maltogenic amylase (MAG1). To enhance enzyme stability and activity retention, immobilization via encapsulation-entrapment is commonly employed, offering biocompatibility and minimizing enzyme loss. Alginate beads are widely used as immobilization matrices; however, their low mechanical strength can result in enzyme leakage. In this study, chitosan was applied as a coating agent to form a stable membrane around alginate beads, improving mechanical integrity. The concentrations of sodium alginate, calcium chloride, and chitosan were optimized using central composite design response surface methodology (CCD-RSM) to maximize enzyme activity recovery. The predicted activity recoveries from the model were 0.044 U/mg for alginate beads and 0.037 U/mg for chitosan-alginate beads, while experimental validation produced slightly higher values of 0.0445 U/mg and 0.048 U/mg, respectively, showing good agreement with the model. Both systems were described by quadratic equations and were statistically significant, with R² values of 0.7751 (alginate) and 0.9171 (chitosan-alginate), indicating superior predictive accuracy for the coated system. These results demonstrate that chitosan coating effectively improves both the mechanical stability and enzyme activity recovery of alginate-based immobilized enzymes, confirming its suitability for enhancing enzyme immobilization performance in biocatalytic applications.