Expression and characterization of a lytic polysaccharide monooxygenase from Bacillus thuringiensis

Expression and characterization of a lytic polysaccharide monooxygenase from Bacillus thuringiensis 1 Introduction</h5> Chitin and cellulose are two most important and highly recalcitrant polysaccharides widely occurring in nature. For an efficient degradation of chitin or cellulose, bacteria generally utilize an enzyme system including nonprocessive endo-type glycoside hydrolases in tandem with processive exo-type glycoside hydrolases [1,2] . Previous studies pointed out that some bacteria produce polysaccharides binding proteins that were capable of increasing substrate accessibility and thus potentiating hydrolytic enzymes [3] . Recent studies highlighted that some of these proteins were capable of catalyzing the cleavage of glycosidic bonds of polysaccharides via an oxidative mechanism, generating a series of oxidized oligosaccharides [4,5] . These bacterial chitin- or cellulose-specific oxidative enzymes are now systematically classified as Auxiliary Activity 10 family (AA10) in the Carbohydrate Active Enzymes (CAZy) database ( www.cazy.org ) [6] . Functionally, AA10 LPMOs can be divided into two subclasses: chitin-oxidative (i.e. Sm CBP21 from Serratia marcescens ) and cellulose-oxidative LPMOs (i.e. CelS2 from Streptomyces coelicolor A3(2)) [7] .</P>Based on genome information, the occurrence of lpmo genes has been confirmed in many chitinolytic and cellulolytic bacteria. It remains to be elucidated whether most of these putative LPMOs have oxidative activities, their large number, however, emphasizes the importance of their http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png International Journal of Biological Macromolecules Elsevier

Expression and characterization of a lytic polysaccharide monooxygenase from Bacillus thuringiensis

Loading next page...
 
/lp/elsevier/expression-and-characterization-of-a-lytic-polysaccharide-xe03hKerU0
Publisher
Elsevier
Copyright
Copyright © 2015 Elsevier B.V.
ISSN
0141-8130
D.O.I.
10.1016/j.ijbiomac.2015.04.054
Publisher site
See Article on Publisher Site

Abstract

1 Introduction</h5> Chitin and cellulose are two most important and highly recalcitrant polysaccharides widely occurring in nature. For an efficient degradation of chitin or cellulose, bacteria generally utilize an enzyme system including nonprocessive endo-type glycoside hydrolases in tandem with processive exo-type glycoside hydrolases [1,2] . Previous studies pointed out that some bacteria produce polysaccharides binding proteins that were capable of increasing substrate accessibility and thus potentiating hydrolytic enzymes [3] . Recent studies highlighted that some of these proteins were capable of catalyzing the cleavage of glycosidic bonds of polysaccharides via an oxidative mechanism, generating a series of oxidized oligosaccharides [4,5] . These bacterial chitin- or cellulose-specific oxidative enzymes are now systematically classified as Auxiliary Activity 10 family (AA10) in the Carbohydrate Active Enzymes (CAZy) database ( www.cazy.org ) [6] . Functionally, AA10 LPMOs can be divided into two subclasses: chitin-oxidative (i.e. Sm CBP21 from Serratia marcescens ) and cellulose-oxidative LPMOs (i.e. CelS2 from Streptomyces coelicolor A3(2)) [7] .</P>Based on genome information, the occurrence of lpmo genes has been confirmed in many chitinolytic and cellulolytic bacteria. It remains to be elucidated whether most of these putative LPMOs have oxidative activities, their large number, however, emphasizes the importance of their

Journal

International Journal of Biological MacromoleculesElsevier

Published: Aug 1, 2015

References

  • Biochemistry
    Forsberg, Z.; Røhr, A.K.; Mekasha, S.; Andersson, K.K.; Eijsink, V.G.H.; Vaaje-Kolstad, G.; Sørlie, M.

You’re reading a free preview. Subscribe to read the entire article.


DeepDyve is your
personal research library

It’s your single place to instantly
discover and read the research
that matters to you.

Enjoy affordable access to
over 18 million articles from more than
15,000 peer-reviewed journals.

All for just $49/month

Explore the DeepDyve Library

Search

Query the DeepDyve database, plus search all of PubMed and Google Scholar seamlessly

Organize

Save any article or search result from DeepDyve, PubMed, and Google Scholar... all in one place.

Access

Get unlimited, online access to over 18 million full-text articles from more than 15,000 scientific journals.

Your journals are on DeepDyve

Read from thousands of the leading scholarly journals from SpringerNature, Elsevier, Wiley-Blackwell, Oxford University Press and more.

All the latest content is available, no embargo periods.

See the journals in your area

DeepDyve

Freelancer

DeepDyve

Pro

Price

FREE

$49/month
$360/year

Save searches from
Google Scholar,
PubMed

Create lists to
organize your research

Export lists, citations

Read DeepDyve articles

Abstract access only

Unlimited access to over
18 million full-text articles

Print

20 pages / month

PDF Discount

20% off