Source:http://linkedlifedata.com/resource/pubmed/id/14543440
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
2003-10-10
|
pubmed:abstractText |
Tissue maceration was generally elucidated by the action of endo-polygalacturonase and endo-pectate or -pectin lyase (endo-PAL or -PNL). In a process of screening of Erwinia and Pseudomonas strains for enzymatic pulping of pectocellulosic bast fibers, it was found that their PAL productivity was not completely related with defibration activity, i.e., the fact that an E.chrysanthemi strain showed high PAL productivity but possessed rather low defibration activity. Moreover, defibration activity was parallel to the amount of neutral sugars released during pulping. Based on these fact, the maceration or enzymatic pulping of basts was estimated to proceed not only by cleavage of interfiber bonding cause by PAL action but also another factors. Among three possibilities proposed on the maceration mechanism of basts, it was elucidated by a concerted action of PAL and PNL with an aid of xylanase. In addition, a quantitative determinative method of maceration activity toward basts was also presented.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:status |
PubMed-not-MEDLINE
|
pubmed:issn |
0734-9750
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
6
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
29-37
|
pubmed:dateRevised |
2006-7-7
|
pubmed:year |
1988
|
pubmed:articleTitle |
Approach to maceration mechanism in enzymatic pulping of bast fibers by alkalophilic pectinolytic enzymes produced by Erwinia species.
|
pubmed:affiliation |
Government Industrial Research Institute, Shikoku, 2-3-3, Hananomiya-chô, Takamatsu 761, Japan.
|
pubmed:publicationType |
Journal Article
|