Purification and characterization of xylanases from Trichoderma inhamatum

By L. A. O. Silva, C. R. Terrasan, E. C. Carmona. 2015

100 citations recorded by the source corpus.

Normal 0 21 false false false PT-BR JA X-NONE 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 Hg 2+ and the detergent SDS strongly reduced the activity while 1,4-dithiothreitol stimulated both enzymes. The xylanases showed specificity for xylan, K m and V max 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. /* Style Definitions */ table.MsoNormalTable {mso-style-name:"Tabla normal"; mso-tstyle-rowband-size:0; mso-tstyle-colband-size:0; mso-style-noshow:yes; mso-style-priority:99; mso-style-parent:""; mso-padding-alt:0cm 5.4pt 0cm 5.4pt; mso-para-margin:0cm; mso-para-margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:12.0pt; font-family:"Times New Roman","serif"; mso-ansi-language:PT-BR; mso-fareast-language:PT-BR;} Background: Results: Conclusions:

Subfields: Biomedical Engineering, Nutrition and Dietetics

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