2009
DOI: 10.1271/bbb.80731
|View full text |Cite
|
Sign up to set email alerts
|

Substrate-Binding Site of Family 11 Xylanase fromBacillus firmusK-1 by Molecular Docking

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
2

Citation Types

0
11
0

Year Published

2010
2010
2021
2021

Publication Types

Select...
10

Relationship

1
9

Authors

Journals

citations
Cited by 38 publications
(11 citation statements)
references
References 39 publications
0
11
0
Order By: Relevance
“…Arabinoxylans are the predominant NSP in wheat and barley ( Izydorczyk and Dexter, 2008 ). Xylanases cleave the internal glycosidic linkages in xylan, producing short-chain xylo-oligosaccharides ( XOS ) ( Jommuengbout et al., 2009 ). These XOS can be utilised more efficiently by gut microbiota, having a direct impact on the overall energy utilisation of cereals.…”
Section: Introductionmentioning
confidence: 99%
“…Arabinoxylans are the predominant NSP in wheat and barley ( Izydorczyk and Dexter, 2008 ). Xylanases cleave the internal glycosidic linkages in xylan, producing short-chain xylo-oligosaccharides ( XOS ) ( Jommuengbout et al., 2009 ). These XOS can be utilised more efficiently by gut microbiota, having a direct impact on the overall energy utilisation of cereals.…”
Section: Introductionmentioning
confidence: 99%
“…These negative effects can be combatted by supplementing the diet with endo-β1, 4-xylanases, which hydrolyses the xylan backbone. These enzymes cleave the internal β-xylosidic glycosidic linkages uninterrupted by side chains to short-chain xylans or xylo-oligosaccharides ( Jommuengbout et al., 2009 ), resulting in a mixture of low-molecular weight xylans, arabinose-substituted xylo-oligosaccharides (arabinoxylan-oligosaccharides, AXOS) and non-substituted xylo-oligosaccharides (XOS). Partial depolymerisation of AX by enzymes reduces molecular chains containing more than 5,000 sugars to just over 1,000 sugars.…”
Section: Introductionmentioning
confidence: 99%
“…However, endo-1,4β-xylanases (gene loci; CT4_03195 and CT4_04894), the main enzymes to attack the xylan backbone of strain CT4 T could not find the CBM. To explain how those xylanases were able to degrade xylan in cassava pulp, the enzymes might have other substrate-binding regions which are located at a certain distance from the active site and are called secondary xylan-binding sites (SXS), which function similarly to the CBM (Jommuengbout et al, 2009). Based on the amino acid sequence alignment of endo-1,4-β-xylanase (CT4_04894) with an endo-1,4-β-xylanase in the glycoside hydrolase family 10 (Xyn10) from Penicillium simplicissimum, which is capable of binding to insoluble xylan via the SXS, it was found that the residues E60, N61, K64, H97, W101, N142, E143, Y187, Q218, H220, E250, W283 and W291 of an endo-1,4-β-xylanase from strain CT4 T (CT4_04894) were conserved with the SXS of Xyn10 from P. simplicissimum (Schmidt, Gübitz & Kratky, 1999).…”
Section: Discussionmentioning
confidence: 99%