Identification and characterization of a novel glucomannanase from Paenibacillus polymyxa
Konjac glucomannan oligosaccharide has attracted much attention due to its broad biological activities. Specific glucomannan degrading enzymes are effective tools for the production of oligosaccharides from konjac glucomannan. However, there are still few reports of commercial enzymes that can speci...
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Published in | 3 Biotech Vol. 11; no. 3; p. 129 |
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Main Authors | , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Cham
Springer International Publishing
01.03.2021
Springer Nature B.V |
Subjects | |
Online Access | Get full text |
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Summary: | Konjac glucomannan oligosaccharide has attracted much attention due to its broad biological activities. Specific glucomannan degrading enzymes are effective tools for the production of oligosaccharides from konjac glucomannan. However, there are still few reports of commercial enzymes that can specifically degrade konjac glucomannan. The gene
ppgluB
encoding a glucomannanase consisting of 553 amino acids (61.5 kDa) from
Paenibacillus polymyxa
3–3 was cloned and heterologous expressed in
Escherichia coli
BL21 (DE3). The recombinant
Pp
GluB showed high specificity for the degradation of konjac glucomannan. Moreover, the hydrolytic products of
Pp
GluB degrade konjac glucomannan were a series of oligosaccharides with degrees of polymerisation of 2–12. Furthermore, the biochemical properties indicated that
Pp
GluB is the optimal active at 45 to 55 °C and pH 5.0–6.0, and shows highly pH stability over a very broad pH range. The present characteristics indicated that
Pp
GluB is a potential tool to be used to produce oligosaccharides from konjac glucomannan. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 2190-572X 2190-5738 |
DOI: | 10.1007/s13205-021-02676-0 |