Abstract
A partially purified β-fructofuranosidase from Aspergillus japonicus was covalently immobilized on to chitosan beads using either glutaraldehyde or tris(hydroxymethyl)phosphine (THP) as a coupling agent. Compared with the glutaraldehyde-immobilized and the free enzyme, the THP-immobilized enzyme had the highest thermal stability with 78% activity retained after 12 days at 37 ° C. The THP-immobilized enzyme also had higher reusability than that immobilized by glutaraldehyde, 75% activity was retained after 11 batches (or 11 days) at 37° C for the THP immobilized enzyme system. Less yield (48%) of fructooligosaccharides (FOS) were produced by the THP-immobilized enzyme compared with the free enzyme system (58%) from 50 (w/v) sucrose at 50 ° C.
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Cheng, TC., Duan, KJ. & Sheu, DC. Immobilization of β-fructofuranosidase from Aspergillus japonicus on chitosan using tris(hydroxymethyl)phosphine or glutaraldehyde as a coupling agent. Biotechnol Lett 27, 335–338 (2005). https://doi.org/10.1007/s10529-005-0984-x
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DOI: https://doi.org/10.1007/s10529-005-0984-x