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Combined strategies for improving the heterologous expression of a novel xylanase from Fusarium oxysporum Fo47 in Pichia pastoris
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作者 Chun Liu Yaping Zhang +3 位作者 Chunting Ye Fengguang Zhao Yian Chen shuangyan han 《Synthetic and Systems Biotechnology》 SCIE CSCD 2024年第3期426-435,共10页
Xylanase,an enzyme capable of hydrolyzing non-starch polysaccharides found in grain structures like wheat,has been found to improve the organizational structure of dough and thus increase its volume.In our past work,o... Xylanase,an enzyme capable of hydrolyzing non-starch polysaccharides found in grain structures like wheat,has been found to improve the organizational structure of dough and thus increase its volume.In our past work,one promising xylanase FXYL derived from Fusarium oxysporum Fo47 and first expressed 779.64 U/mL activity in P.pastoris.It has shown significant potential in improving the quality of whole wheat bread,making it become a candidate for development as a new flour improver.After optimization of expression elements and gene dose,the xylanase activity of FXYL strain carrying three-copies reached 4240.92 U/mL in P.pastoris.In addition,12 factors associated with the three stages of protein expression pathway were co-expressed individually in order in three-copies strain,and the translation factor Pab1 co-expression increased FXYL activity to 8893.53 U/mL.Nevertheless,combining the most effective or synergistic factors from three stages did not exhibit better results than co-expressing them alone.To further evaluate the industrial potential,the xylanase activity and protein concentration reached 81184.51 U/mL and 11.8 g/L in a 5 L fed-batch fermenter.These engineering strategies improved the expression of xylanase FXYL by more than 104-fold,providing valuable insights for the cost-effective industrial application of FXYL in the baking field. 展开更多
关键词 XYLANASE Pichia pastoris Heterologous protein Secretion expression
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