Vasimon RuanglekRutchadaporn SriprangNakul RatanaphanPacawadee TirawongsarojDuriya ChantasighSutipa TanapongpipatKusol PootanakitLily EurwilaichitrThailand National Center for Genetic Engineering and BiotechnologyMahidol University2018-08-242018-08-242007-07-02Enzyme and Microbial Technology. Vol.41, No.1-2 (2007), 19-25014102292-s2.0-34248385655https://repository.li.mahidol.ac.th/handle/20.500.14594/24165A recombinant gene XylB (564 bp) encoding endo-1,4-β-xylanase, obtained from Aspergillus niger BCC14405, was successfully cloned and secreted as a 21 kDa in Pichia pastoris under the control of AOX1 promoter. The activity of the recombinant xylanase was highest at 55 °C which was 5 °C higher than native xylanase. In addition, the recombinant xylanase was active over the range of pH 3.6-6.5 with maximal activity at pH 5 (8007 U/mg). When compared to a commercial enzyme, in vitro digestibility of the recombinant enzyme was 1.8- and 2.4-folds higher digesting rates of rice bran and soybean meal fibers, respectively. Two-liter production of xylanase was performed with BSM medium which increased cell concentration up to 84.5 gdry-weight/L via the 80% μmaxexponential feed strategy. This process provided maximum xylanase production (3676 U/mL) with highest specific activity (7352 U/mgprotein) and volumetric productivity (22,832 U/L/h) at 3.0% (v/v) methanol induction. By far, this was the highest xylanase expression in P. pastoris host system being reported. Thus, this BCC14405 recombinant xylanase could be produced and used effectively as a feed additive for animals. © 2006 Elsevier Inc. All rights reserved.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyImmunology and MicrobiologyArticleSCOPUS10.1016/j.enzmictec.2006.11.019