rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
2-3
|
pubmed:dateCreated |
2001-8-13
|
pubmed:abstractText |
Desized cotton fabric and cotton seed-coat fragments (impurities) have been treated with commercial cellulase (Celluclast 1.5 L), hemicellulase-pectinase (Viscozyme 120 L) and xylanase (Pulpzyme HC) enzymes. Seed-coat fragments hydrolyzed much faster than the cotton fabric itself. This relative difference in hydrolysis rates makes possible a direct enzymatic removal of seed-coat fragments from desized cotton fabric. Addition of chelating agents such as ethylenediamine-tetra-acetic acid (EDTA) markedly enhanced the directed enzyme action. Pretreatments carried out in acidic solution at pH 5 increased the lightness of seed-coat fragments, contrary to the samples treated in neutral medium at pH 7. Alkaline scouring resulted in darker seed-coat fragments except for the samples pretreated with Pulpzyme HC plus EDTA. This effect is similar to that observed in the biobleaching process in pulp and paper industry.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
0168-1656
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
23
|
pubmed:volume |
89
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
271-9
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:11500222-Calcium,
pubmed-meshheading:11500222-Cellulase,
pubmed-meshheading:11500222-Chelating Agents,
pubmed-meshheading:11500222-Edetic Acid,
pubmed-meshheading:11500222-Glycoside Hydrolases,
pubmed-meshheading:11500222-Gossypium,
pubmed-meshheading:11500222-Hydrolysis,
pubmed-meshheading:11500222-Polygalacturonase,
pubmed-meshheading:11500222-Seeds,
pubmed-meshheading:11500222-Xylan Endo-1,3-beta-Xylosidase,
pubmed-meshheading:11500222-Xylosidases
|
pubmed:year |
2001
|
pubmed:articleTitle |
Enzymes and chelating agent in cotton pretreatment.
|
pubmed:affiliation |
Budapest University of Technology and Economics, PO Box 91, H-1521, Budapest, Hungary. emi.oct@chem.bme.hu
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|