[Improvement of recombinant xylanase XynF1 from Aspergillus oryzae expressed in Pichia pastoris by site-directed mutagenesis].
The recombinant xylanase XynF1 from Aspergillus oryzae expressed in the methylotrophic yeast Pichia pastoris was improved by site-directed mutagenesis. The mutant I156A secreted about 47.7 U/mL xylanase XynF1 in the BMMY medium. The mutant xylanase XynF1 was purified by ion exchange and gel filtration chromatographies. The molecular weight of purified XynF1 was 35 kD. XynF1 was stable between pH 4-9 and its optimum pH was 7.0. The optimum temperature of XynF1 was 45 degrees C and it was stable below 50 degrees C. The properties of mutant were same as the parent's except the stability of temperature.
Lu
Jian
J
School of Biotechnology, Key Laboratory of Industry Biotechnology Under Ministry of Education, Souhern Yangtze University, Wuxi 214036, China.
Cao
Yu
Y
Chen
Jian
J
D001236:Aspergillus oryzae / Q000201:enzymology / Q000235:genetics*; D043364:Endo-1,4-beta Xylanases / Q000096:biosynthesis* / Q000235:genetics / Q000302:isolation & purification; D015966:Gene Expression Regulation, Fungal; D005800:Genes, Fungal; D016297:Mutagenesis, Site-Directed; D010843:Pichia / Q000201:enzymology* / Q000235:genetics; D011401:Promoter Regions, Genetic; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics
D011994:Recombinant Proteins; D043364:Endo-1,4-beta Xylanases