Linked Life Data

15450181

Source:http://linkedlifedata.com/resource/pubmed/id/15450181

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2004-9-28
pubmed:abstractText
The filamentous fungus Penicillium funiculosum produces a mixture of modular and non-modular xylanases belonging to different glycoside hydrolase (GH) families. In the present study, we heterologously expressed the cDNA encoding GH11 xylanase B (XYNB) and studied the enzymatic properties of the recombinant enzyme. Expression in Escherichia coli led to the partial purification of a glutathione fusion protein from the soluble fraction whereas the recombinant protein produced in Pichia pastoris was successfully purified using a one-step chromatography. Despite O-glycosylation heterogeneity, the purified enzyme efficiently degraded low viscosity xylan [K(m)=40+/-3 g l(-1), V(max)=16.1+/-0.8 micromol xylose min(-1) and k(cat)=5405+/-150 s(-1) at pH 4.2 and 45 degrees C] and medium viscosity xylan [K(m)=34.5+/-3.2 g l(-1), V(max)=14.9+/-1.0 micromol xylose min(-1)k(cat)=4966+/-333 s(-1) at pH 4.2 and 45 degrees C]. XYNB was further tested for its ability to interact with wheat xylanase inhibitors. The xylanase activity of XYNB produced in P. pastoris was strongly inhibited by both XIP-I and TAXI-I in a competitive manner, with a K(i) of 89.7+/-8.5 and 2.9+/-0.3 nM, respectively, whereas no inhibition was detected with TAXI-II. Physical interaction of both TAXI-I and XIP-I with XYNB was observed using titration curves across a pH range 3-9.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
1701
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
121-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
The inhibition specificity of recombinant Penicillium funiculosum xylanase B towards wheat proteinaceous inhibitors.
pubmed:affiliation
Laboratoire de Biochimie et Biologie de la Nutrition, Institut Méditerranéen de Recherche en Nutrition, UMR Université Aix Marseille III-INRA 1111, Service 342, Faculté des Sciences et Techniques Saint-Jérôme, 13397 Marseille Cedex 20, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't