A novel thermoacidophilic family 10 xylanase from Penicillium pinophilum C1

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• 作者：Hongying  ; Cai¹ ; Pengjun  ; Shi¹ ; Yingguo  ; Bai ; Huoqing  ; Huang ; Tiezheng  ; Yuan ; Peilong  ; Yang ; Huiying  ; Luo ; Kun  ; Meng ; Bin  ; Yao  ; ;   ; ^{yaobin@mail.caas.net.cn} ;   ; ^{yaobin@caas-bio.net.cn}
• 关键词：Penicillium pinophilum C1 ; Xylanase ; Thermoacidophilic ; Pichia pastoris ; Malting and brewing
• 刊名：Process Biochemistry
• 出版年：2011
• 出版时间：December 2011
• 年：2011
• 卷：46
• 期：12
• 页码：2341-2346
• 全文大小：503 K

文摘

A novel endo-¦Â-1,4-xylanase gene (xyn10C1) was cloned from Penicillium pinophilum C1 and overexpressed in Pichia pastoris. The 1071-bp full-length gene encodes a 356-residue polypeptide containing the catalytic domain of glycoside hydrolase 10. Deduced XYN10C1 shares highest amino acid sequence identity of 49.3 % with a putative xylanase from Glomeella graminicola M1.001. Purified recombinant XYN10C1 showed maximal activity at pH 4.0?.5 and 75 ¡ãC, exhibited good adaptability to broad acidic pH and temperature ranges (>69.0 % activity at pH 2.5?.5; and >91.0 % activity at 70?0 ¡ãC and 22.2 % even at 90 ¡ãC), and was highly stable at pH 2.0?.0 for 1 h at 37 ¡ãC. The specific activity, K_m and V_max values for birchwood xylan and soluble wheat arabinoxylan were 100.7 and 137.4 U/mg, 4.3 and 6.9 mg/ml, and 195.4 and 209.3 ¦Ìmol/min/mg, respectively. The enzyme was strongly resistant to most metal ions and proteases (pepsin and trypsin). Under simulated mashing conditions, addition of XYN10C1 (80 U) to the brewery mash (12.5 g in 50 ml system) significantly increased the filtration rate by 26.7 % and reduced the viscosity by 9.8 % , respectively. All these favorable enzymatic properties make XYN10C1 attractive for potential applications in the food and animal feed industries.