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Operational stability of immobilized sucrose phosphorylase: Continuous production of α-glucose-1-phosphate at elevated temperatures

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논문

Operational stability of immobilized sucrose phosphorylase: Continuous production of α-glucose-1-phosphate at elevated temperatures

학술지

Process biochemistry

저자명

De Winter, K.; Cerdobbel, A.; Soetaert, W.; Desmet, T.

초록

Sucrose phosphorylase (SP) is a useful biocatalyst for the selective transfer of &alpha;-glucosyl residues to a variety of acceptor molecules. Its industrial application is, however, hampered by the lack of enzyme variants that can withstand the process temperature of 60<SUP>o</SUP>C. We have recently shown that the stability of the SP from Bifidobacterium adolescentis can be improved by immobilization on Sepabeads EC-HFA, and have now applied this biocatalyst for the continuous production of &alpha;-d-glucose-1-phosphate from sucrose. To lower the costs, the enzyme has only been partially purified prior to immobilization. Interestingly, the presence of substrate was found to dramatically enhance the stability of the biocatalyst, allowing its use in a packed-bed reactor for more than 2 weeks at 60<SUP>o</SUP>C without loss of activity. The overall process generated a space-time yield of 179g/l/h, and the product could be recovered in crystalline form with a yield of 86%.

발행연도

2011

발행기관

Elsevier Applied Science

ISSN

1359-5113

46

10

페이지

pp.2074-2078

주제어

Sucrose phosphorylase; Immobilization; Sepabeads; Alfa-d-glucose-1-phosphate; Stabilization; Production

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논문; 2011-10-01

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