Abstract
The genes for dextransucrase and dextranase were cloned from the genomic regions of Leuconostoc mesenteroides MTCC 10508 and Streptococcus mutans MTCC 497, respectively. Heterologous expression of genes was performed in Escherichia coli. The purified enzyme fractions were entrapped in the alginate–pectin beads. A high immobilization yield of dextransucrase (~ 96%), and dextranase (~ 85%) was achieved. Alginate–pectin immobilization did not affect the optimum temperature and pH of the enzymes; rather, the thermal tolerance and storage stability of the enzymes was improved. The repetitive batch experiments suggested substantially good operational stability of the co-immobilized enzyme system. The synergistic catalytic reactions of alginate–pectin co-entrapped enzyme system were able to produce 7–10 g L−1 oligosaccharides of a high degree of polymerization (DP 3–9) from sucrose (~ 20 g L−1) containing feedstocks, e.g., table sugar and cane molasses. The alginate–pectin-based co-immobilized enzyme system is a useful catalytic tool to bioprocess the agro-industrial bio-resource for the production of prebiotic biomolecules.
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Acknowledgements
Authors acknowledge the Department of Biotechnology (DBT), Government of India for supporting the present work at Center of Innovative and Applied Bioprocessing (CIAB), Mohali. SPS cordially acknowledges the DBT project-grant, BT/PR17586/PFN/20/1195. MS acknowledges Council of Scientific and Industrial Research (CSIR) for SRF fellowship, and the Department of Food Technology, Guru Jambheshwar University of Science and Technology, Hisar, for Ph.D. registration.
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Sharma, M., Sangwan, R.S., Khatkar, B.S. et al. Alginate–pectin co-encapsulation of dextransucrase and dextranase for oligosaccharide production from sucrose feedstocks. Bioprocess Biosyst Eng 42, 1681–1693 (2019). https://doi.org/10.1007/s00449-019-02164-z
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DOI: https://doi.org/10.1007/s00449-019-02164-z