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- aggregation classification "A1".
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2010".
- aggregation format "application/pdf".
- aggregation hasFormat 1088621.bibtex.
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- aggregation isPartOf urn:issn:1860-6768.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Sucrose phosphorylase as cross-linked enzyme aggregate: improved thermal stability for industrial applications".
- aggregation abstract "Sucrose phosphorylase is an interesting biocatalyst that can glycosylate a variety of small molecules using sucrose as a cheap but efficient donor substrate. The low thermostability of the enzyme, however, limits its industrial applications, as these are preferably performed at 60 degrees C to avoid microbial contamination. Cross-linked enzyme aggregates (CLEAs) of the sucrose phosphorylase from Bifidobacterium adolescentis were found to have a temperature optimum that is 17 degrees C higher than that of the soluble enzyme. Furthermore, the immobilized enzyme displays an exceptional thermostability, retaining all of its activity after 1 week incubation at 60 degrees C. Recycling of the biocatalyst allows its use in at least ten consecutive reactions, which should dramatically increase the commercial potential of its glycosylating activity.".
- aggregation authorList BK494756.
- aggregation endPage "1197".
- aggregation issue "11".
- aggregation startPage "1192".
- aggregation volume "5".
- aggregation aggregates 1184541.
- aggregation isDescribedBy 1088621.
- aggregation similarTo biot.201000202.
- aggregation similarTo LU-1088621.