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Electronic Journal of Biotechnology
Universidad Católica de Valparaíso
ISSN: 0717-3458
Vol. 18, No. 4, 2015, pp. 307-313
Bioline Code: ej15050
Full paper language: English
Document type: Research Article
Document available free of charge

Electronic Journal of Biotechnology, Vol. 18, No. 4, 2015, pp. 307-313

 en Purification and characterization of xylanases from Trichoderma inhamatum check for this species in other resources
Silva, L.A.O.; Terrasan, César Rafael Fanchini & Carmona, Eleonora Cano


Background: Two xylanases, Xyl I and Xyl II, were purified from the crude extracellular extract of a Trichoderma inhamatum check for this species in other resources 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 50°C in pH 5.0–5.5 for Xyl I and 5.5 for Xyl II. The xylanases were very stable at 40°C 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 2680.2 and 462.2 U·mg of protein-1 (Xyl I) and 10.7, 4.0 mg·mL-1 and 4553.7 and 1972.7 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.

Enzyme purification; Physico-chemical properties; Trichoderma inhamatum; Xylanases

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