Inulinase immobilisation in PAA/PEG composite for efficient fructooligosaccharides production
Journal
Biocatalysis and Biotransformation
Date Issued
2020-12-26
Author(s)
Temkov, Mishela
Velickova, Elena
Krastanov, Albert
DOI
10.1080/10242422.2020.1858815
Abstract
Inulinase was immobilised by entrapment method in polyacrylamide/polyethylene glycol composite
and evaluated for its efficiency for short-chain fructooligosaccharides (3–6 degrees of
polymerisation) production in batch hydrolysis system. Aqueous two-phase polymerisation technique
was used to synthesise the composite, where aqueous polyethylene glycol 1000 containing
the enzyme was used as dispersant with ammonium persulfate as initiator. The
characteristics of free and immobilised inulinase were investigated and compared, and the
results showed shift of pH and temperature optimum and change in stability caused by the
immobilisation material. The immobilised preparation retained 50% of its initial activity after 20
successive batch cycles of 1 h each. The conversion degree of highly polymerised inulin to fructooligosaccharides (3–6 degrees of polymerisation) was 36% when using 30% PAA/PEG, w/v.
and evaluated for its efficiency for short-chain fructooligosaccharides (3–6 degrees of
polymerisation) production in batch hydrolysis system. Aqueous two-phase polymerisation technique
was used to synthesise the composite, where aqueous polyethylene glycol 1000 containing
the enzyme was used as dispersant with ammonium persulfate as initiator. The
characteristics of free and immobilised inulinase were investigated and compared, and the
results showed shift of pH and temperature optimum and change in stability caused by the
immobilisation material. The immobilised preparation retained 50% of its initial activity after 20
successive batch cycles of 1 h each. The conversion degree of highly polymerised inulin to fructooligosaccharides (3–6 degrees of polymerisation) was 36% when using 30% PAA/PEG, w/v.
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