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Levanase From Bacillus Subtilis Hydrolyses β-2,6 Fructosyl Bonds in Bacterial Levans and in Grass Fructans

Levanase From Bacillus Subtilis Hydrolyses β-2,6 Fructosyl Bonds in Bacterial Levans and in Grass Fructans

Susanne L Jensen, Mikkel B Diemer, Maria Lundmark, Flemming H Larsen, Andreas Blennow, Helle K Mogensen, Tom H Nielsen

Int J Biol Macromol. 2016 Apr;85:514-21.

PMID: 26773563

Abstract:

A Levanase, LevB, from Bacillus subtilis 168, was expressed as a His6-tagged protein in Escherichia coli. The enzyme was purified and characterised for its activity and substrate specificity. LevB has a pH optimum of 6.0-6.5 and a maximum observed specific activity of 3 U mg(-1) using levan from Erwinia herbicola as substrate. Hydrolysis products were analysed by HPAEC, TLC, and NMR using chicory root inulin, mixed linkage fructans purified from ryegrass (Lolium perenne) and levan from E. herbicola as substrates. This revealed that LevB is an endolevanase that selectively cleaves the (β-2,6) fructosyl bonds and does not hydrolyse inulin. Ryegrass fructans and bacterial levan was hydrolysed partially releasing oligosaccharides, but together with exoinulinase, LevB hydrolysed both ryegrass fructans and bacterial levan to near completion. We suggest that LevB can be used as a tool to achieve more structural information on complex fructans and to achieve complete degradation and quantification of mixed linkage fructans.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9013950	Levan from Erwinia herbicola		9013-95-0	Price

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