How to Cite
Abstract
Background: Two xylanases, Xyl I and Xyl II, were purified from the crude extracellular extract of a Trichoderma inhamatum strain cultivated in liquid medium with oat spelts xylan.
Results: The molecular masses of the purified enzymes estimated by SDS-PAGE and gel filtration were, respectively, 19 and 14 kDa for Xyl I and 21 and 14.6 kDa for Xyl II. The enzymes are glycoproteins with optimum activity at 50ºC in pH 5.0 - 5.5 for Xyl I and 5.5 for Xyl II. The xylanases were very stable at 40ºC and in the pH ranges from 4.5 - 6.5 for Xyl I and 4.0 - 8.0 for Xyl II. The ion Hg2+ and the detergent SDS strongly reduced the activity while 1,4-dithiothreitol stimulated both enzymes. The xylanases showed specificity for xylan, Km and Vmax of 14.5, 1.6 mg ● mL-1 and 2,680.2 and 462.2 U ● mg of protein-1 (Xyl I) and 10.7, 4.0 mg ● mL-1 and 4,553.7 and 1,972.7 U ● mg of protein-1 (Xyl II) on oat spelts and birchwood xylan, respectively. The hydrolysis of oat spelts xylan released xylobiose, xylotriose, xylotetrose and larger xylooligosaccharides.
Conclusions: The enzymes present potential for application in industrial processes that require activity in acid conditions, wide-ranging pH stability, such as for animal feed, or juice and wine industries. Background:Results:
Conclusions:
Upon acceptance of an article by the journal, authors will be asked to transfer the copyright to Electronic Journal of Biotechnology, which is committed to maintain the electronic access to the journal and to administer a policy of fair control and ensure the widest possible dissemination of the information. The author can use the article for academic purposes, stating clearly the following: "Published in Electronic Journal of Biotechnology at DOI:10.2225/volXX-issueX-fulltext-XX".
The Copyright Transfer Agreement must be submitted as a signed scanned copy to biotec@ucv.cl. All authors must send a copy of this document.