2012
DOI: 10.1271/bbb.110605
|View full text |Cite
|
Sign up to set email alerts
|

Cloning and Characterization of a Gene Coding for a Major Extracellular Chitosanase from the Koji MoldAspergillus oryzae

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

1
3
0

Year Published

2014
2014
2024
2024

Publication Types

Select...
7

Relationship

0
7

Authors

Journals

citations
Cited by 7 publications
(4 citation statements)
references
References 13 publications
1
3
0
Order By: Relevance
“…This indicates that the consumption of sulfate is increasing, or even relatively insufficient, which leads to excessive consumption of 34 S in sulfate, resulting in a rapid increase of 34 S in sulfides, usually close to the value of sulfate in seawater. This was a pattern similar to those found in the Nankai Trough and northern SCS, where the occurrence of AOM significantly increase CRS contents and δ 34 S CRS values of the sediments [6,57]. Therefore, the observed high CRS content and δ 34 S CRS values within depths of Unit III may indicate the intensification of AOM–SR and the current and/or past locations of the SMTZ.…”
Section: Discussionsupporting
confidence: 81%
“…This indicates that the consumption of sulfate is increasing, or even relatively insufficient, which leads to excessive consumption of 34 S in sulfate, resulting in a rapid increase of 34 S in sulfides, usually close to the value of sulfate in seawater. This was a pattern similar to those found in the Nankai Trough and northern SCS, where the occurrence of AOM significantly increase CRS contents and δ 34 S CRS values of the sediments [6,57]. Therefore, the observed high CRS content and δ 34 S CRS values within depths of Unit III may indicate the intensification of AOM–SR and the current and/or past locations of the SMTZ.…”
Section: Discussionsupporting
confidence: 81%
“…Identified in KMS cluster 16, which contains >50% of genes encoding CAZymes, An16g00670.Aspni5_127791 showed increased expression on KMS from 9 to 24 h. A Phyre2 HMM-based search for structurally similar proteins [ 48 ] identified similarity to B. subtilis YuiC (PDB 4wjt), which cleaves chitin oligosaccharides, with conservation of the catalytic residue [ 49 ]. The mycoCLAP database for characterised lignocellulolytic enzymes [ 50 ] indicated similarity to the linker and chitosan-binding domain [ 51 ] of GH75 chitosanases. These results suggest that An16g00670.Aspni5_127791 may have chitin or chitosan binding/hydrolysis function.…”
Section: Resultsmentioning
confidence: 99%
“…Among the proteins mainly secreted in the aspersed and immersed BfRs, we observed large quantities of chitosanase (CsnC) and exo-glucanase (ExgA). The chitosanase CsnC catalyzes the cleavage of chitosan, the deacetylated form of the chitin polymer, a component of fungal cell walls (Sugita et al 2012). The exo-glucanase (ExgA) is responsible for the hydrolysis of the glucosidic bond found in β-1-3-glucan, a component of fungal cell walls.…”
Section: -D Gel Characterizationmentioning
confidence: 99%