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1¡¢ The problem faced by the xylanases using in pulp and paper industry, however, is retaining active under the extreme process condition of high temperature and high alkali. 2¡¢All the positive mutants were detected by their ability to produce a hydrolysis zone on xylan plates (LB-Agar plate added 1% xylan, 100 ¦Ìg/mL ampicillin, and 1mM IPTG, pH 7.0), then were transfered to alkali xylan plates which at pH 10.0 for the products of the first ground epPCR and pH 11.0 for the products of the second ground epPCR. 3¡¢Collected the clones revealing relative higher xylanase activity compared with that of E. coli BL21 (pET-XynG1-1) for further enzymatic properties studying and gene sequencing. 4¡¢ The results in Table 4 showed that both XynG1-1 and XynG1-1B43cc pretreatment indicated distinct effect in the bleaching of cotton stalk pulp. 5¡¢XynG1-1 and XynG1-1B43cc pretreatment gained brightness levels of 73.39% and 78.95% which revealed obvious higher than that (69.66%) of control (Table 4). 6¡¢All of the results indicated that the mutant xylanase XynG1-1B43cc is more available to the high temperature and high alkali process condition of paper industry. |
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1¡¢ The problem faced by the xylanases used in pulp and paper industry, however, is retaining active under the extreme process condition of high temperature and high alkali. 2¡¢All the positive mutants were detected by their ability to produce a hydrolysis zone on xylan plates (LB-Agar plate added 1% xylan, 100 ¦Ìg/mL ampicillin, and 1mM IPTG, pH 7.0), and then to be transferred to alkali xylan plates, at pH 10.0 for the products of the first ground epPCR and pH 11.0 for those of the second. ×¢£ºÕâÀïÎÒÀí½â to produce ºÍ to be transferred²¢ÁУ¬¹²Í¬À´ÐÞÊÎability¡£Èç¹ûÂß¼²»¶Ô, transferred ...ÊǺÍwere detected ...²¢ÁеÄ,ÄÇôÕâ¾ä»°¾ÍÓ¦¸Ã¸Ä³É£º All the positive mutants were detected by their ability to produce a hydrolysis zone on xylan plates (LB-Agar plate added 1% xylan, 100 ¦Ìg/mL ampicillin, and 1mM IPTG, pH 7.0), and were then transferred to alkali xylan plates, at pH 10.0 for the products of the first ground epPCR and pH 11.0 for those of the second. 3¡¢The collected clones revealed relatively higher xylanase activity compared with that of E. coli BL21 (pET-XynG1-1), which requires further enzymatic property study and gene sequencing. ×¢£ºÕâÀïǰ°ë¾äºÍºó±ßµÄËÆºõûʲôÁ¬½Ó£¬ÕâÀï¼ÙÉèǰ°ë¾ä˵µÄÇé¿öÐèÒªurther enzymatic property study and gene sequencing£¬Èç¹û²»Êǵϰ£¬ÇëÖ¸³öÈ·ÇÐÂß¼¹ØÏµ 4¡¢ The results in Table 4 showed that both XynG1-1 and XynG1-1B43cc pretreatment had distinct effects on bleaching of cotton stalk pulp. 5¡¢By XynG1-1 and XynG1-1B43cc pretreatment brightness levels of 73.39% and 78.95% were obtained, which are obviously higher than that (69.66%) of the control one (Table 4). 6¡¢All the results indicated that the mutant xylanase XynG1-1B43cc is more tolerant to the high temperature and high alkali process condition of paper industry than others¡£ ×¢£º´ÓÉÏÎÄÀí½âmutant xylanase XynG1-1B43cc¶ÔÓÚhigh temperature and high alkali process condition of paper industryÓ¦¸ÃÊDZȽϲ»Ãô¸Ð¡¢²»´óÊÜÓ°ÏìµÄ£¬ËùÒÔÓÃÁËtolerant¡£ÔÒëÎÄis more availableÒÉËÆÏë˵mutant xylanase XynG1-1B43cc¶ÔÓÚ¸ßΡ£¡£¡£¸üºÃÓ㬵«available²»Íס£ÁíÍâÓñȽϼ¶µ«Ã»Óб»±È½Ï¶ÔÏó¡£ÎÒÓÃÁËthan others,Æäʵ²»¹»È·¶¨£¬»¹ÇëÂ¥Ö÷Õå×õ½µ×ÏëºÍʲô±È£¬ È»ºó´úÌæ"others" ²»ÊÇרҵÄÚÐУ¬²»Í×¼ûÁ |

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