A new bioprocess for the production of prebiotic lactosucrose by an immobilized β-galactosidase
[Display omitted] •β-galactosidase from Bacillus circulans was immobilized on chitosan macroparticles.•A new bioprocess for lactosucrose synthesis was developed.•Reaction conditions can modulate the product synthesis.•The immobilized enzyme could be used for 30 reaction cycles. A new bioprocess for...
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Published in | Process biochemistry (1991) Vol. 55; pp. 96 - 103 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Barking
Elsevier Ltd
01.04.2017
Elsevier BV |
Subjects | |
Online Access | Get full text |
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Summary: | [Display omitted]
•β-galactosidase from Bacillus circulans was immobilized on chitosan macroparticles.•A new bioprocess for lactosucrose synthesis was developed.•Reaction conditions can modulate the product synthesis.•The immobilized enzyme could be used for 30 reaction cycles.
A new bioprocess for the synthesis of lactosucrose was studied using a covalently immobilized β-galactosidase on macrospheres of chitosan. The effects of temperature and pH on the production of lactosucrose and other oligosaccharides were evaluated. At 30°C and pH 7.0, the maximum concentration of lactosucrose reached to 79gL−1. The change of the reaction conditions allowed to modify the qualitative profile of the final products without quantitative change in the total of oligosaccharides produced. At pH 7 and 30°C, products profile was 79gL−1 of lactosucrose, 37gL−1 of galactooligosaccharides and 250gL−1 of total oligosaccharides, while at pH 5 and 64°C the concentrations for the same compounds were 40, 62 and 250gL−1, respectively. The immobilization increased the thermal stability up to 260-fold. Using 300gL−1 of sucrose and 300gL−1 of lactose, and 8.5mg of chitosan mL−1, 30 cycles of reuse were performed and the biocatalyst kept the maximal lactosucrose synthesis. These results fulfill some important aspects for the enzyme immobilization and oligosaccharides synthesis: the simplicity of the protocols, the high operational stability of the enzyme and the possibility of driving the final products. |
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ISSN: | 1359-5113 1873-3298 |
DOI: | 10.1016/j.procbio.2017.01.015 |