Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
23
pubmed:dateCreated
2010-11-22
pubmed:abstractText
Enzymatic lignocellulose hydrolysis plays a key role in microbially driven carbon cycling and energy conversion and holds promise for bio-based energy and chemical industries. Cellulases (key lignocellulose-active enzymes) are prone to interference from various noncellulosic substances (e.g., metal ions). During natural cellulolysis, these substances may arise from other microbial activities or abiotic events, and during industrial cellulolysis, they may be derived from biomass feedstocks or upstream treatments. Knowledge about cellulolysis-inhibiting reactions is of importance for the microbiology of natural biomass degradation and the development of biomass conversion technology. Different metal ions, including those native to microbial activity or employed for biomass pretreatments, are often tested for enzymatic cellulolysis. Only a few metal ions act as inhibitors of cellulases, which include ferrous and ferric ions as well as cupric ion. In this study, we showed inhibition by ferrous/ferric ions as part of a more general effect from oxidative (or redox-active) metal ions and their complexes. The correlation between inhibition and oxidation potential indicated the oxidative nature of the inhibition, and the dependence on air established the catalytic role that iron ions played in mediating the dioxygen inhibition of cellulolysis. Individual cellulases showed different susceptibilities to inhibition. It is likely that the inhibition exerted its effect more on cellulose than on cellulase. Strong iron ion chelators and polyethylene glycols could mitigate the inhibition. Potential microbiological and industrial implications of the observed effect of redox-active metal ions on enzymatic cellulolysis, as well as the prevention and mitigation of this effect in industrial biomass conversion, are discussed.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/20889796-12209002, http://linkedlifedata.com/resource/pubmed/commentcorrection/20889796-12646708, http://linkedlifedata.com/resource/pubmed/commentcorrection/20889796-14758556, http://linkedlifedata.com/resource/pubmed/commentcorrection/20889796-15304785, http://linkedlifedata.com/resource/pubmed/commentcorrection/20889796-16142468, http://linkedlifedata.com/resource/pubmed/commentcorrection/20889796-16205911, http://linkedlifedata.com/resource/pubmed/commentcorrection/20889796-16650812, http://linkedlifedata.com/resource/pubmed/commentcorrection/20889796-17289988, http://linkedlifedata.com/resource/pubmed/commentcorrection/20889796-18259168, http://linkedlifedata.com/resource/pubmed/commentcorrection/20889796-18338189, http://linkedlifedata.com/resource/pubmed/commentcorrection/20889796-18371173, http://linkedlifedata.com/resource/pubmed/commentcorrection/20889796-18497287, http://linkedlifedata.com/resource/pubmed/commentcorrection/20889796-18548623, http://linkedlifedata.com/resource/pubmed/commentcorrection/20889796-19502046, http://linkedlifedata.com/resource/pubmed/commentcorrection/20889796-19523812, http://linkedlifedata.com/resource/pubmed/commentcorrection/20889796-19581085, http://linkedlifedata.com/resource/pubmed/commentcorrection/20889796-20154118, http://linkedlifedata.com/resource/pubmed/commentcorrection/20889796-3115960, http://linkedlifedata.com/resource/pubmed/commentcorrection/20889796-5031119, http://linkedlifedata.com/resource/pubmed/commentcorrection/20889796-7640890, http://linkedlifedata.com/resource/pubmed/commentcorrection/20889796-8507185, http://linkedlifedata.com/resource/pubmed/commentcorrection/20889796-8661329, http://linkedlifedata.com/resource/pubmed/commentcorrection/20889796-9291624, http://linkedlifedata.com/resource/pubmed/commentcorrection/20889796-9335167, http://linkedlifedata.com/resource/pubmed/commentcorrection/20889796-9758774
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1098-5336
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
76
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7673-82
pubmed:dateRevised
2011-7-28
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Inhibition of cellulase-catalyzed lignocellulosic hydrolysis by iron and oxidative metal ions and complexes.
pubmed:affiliation
Novozymes, Inc., 1445 Drew Avenue, Davis, CA 95618, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.