摘要
研究了玉米秸秆在储存过程中质外体蛋白含量的变化情况,及其对Penicilllumexpansum纤维素酶活力的影响。结果表明随着储存时间的延长,可抽提的玉米秸秆质外体蛋白的数量逐渐减少,与P.expansum纤维素酶的协同作用也随之减弱。储存玉米秸秆质外体蛋白没有内源性纤维素酶活力,而新鲜玉米秸秆有内源性EG活性,但它的稳定性较差,储存半年后基本降解或失活。储存秸秆质外体蛋白对FPA酶活力、棉花酶活力、β-葡萄糖苷酶活力有明显的增效作用,最大增效分别达到95.32%、102.06%和96.6%。而对CMCase却表现出抑制作用,最大抑制率为49.52%,质外体蛋白-EG-βG表现出明显的协同关系,而它对CBH酶活力没有影响。消除内源性EG的影响后,新鲜玉米秸质外体蛋白对FPA活力、棉花酶活力、β-葡萄糖苷酶活力的促进率,以及CMCase的抑制率均高于储存秸秆的质外体蛋白。可见质外体蛋白是天然纤维素酶解研究不可忽视的影响因素。
We studied the alteration of the maize straw apoplast proteins in the process of preservation, and analyzed the effects of apoplast proteins on Penicillum expansum cellulase activities. The results show that： the extractable apoplast proteins are gradually decreased during the preservation of maize straw. Meanwhile, their synergistic effects on P. expensum cellulose are also attenuated. The apoplast proteins extracted from fresh maize straw possess endogenous EG activities, which is unstable and completely vanished after 6 months preservation. The apoplast proteins from the preserved straw exhibit significant synergistic effect on FPA, cotton lyase and β-glucosidase. The maximal synergistic values are 95.32%, 102.06% and 96.6%, respectively. But interestingly, they inhibit the CMCase activity （max. 49.52% ）. Apoplast proteins show distinctive synergy with βG and EG, but have no effect on CBH activity. After eliminating the effect of endogenous EG, the apoplast proteins from fresh maize straw have enhanced synergistic or inhibiting effects on FPA, Cotton lyase, βG and CMCase than those extracted from the preserved straw. Based on our observation, the apoplast proteins play important roles in regulating the cellulase activities. The detailed analysis of the related mechanisms will greatly benefit the studies of the natural biomaterials hydrolysis.
出处
《生物工程学报》
CAS
CSCD
北大核心
2006年第2期257-262,共6页
Chinese Journal of Biotechnology
基金
国家重点基础研究发展计划项目(No.2004CB71700)
中国科学院知识创新项目(No.KJCXZ-SW-206-2)。~~
关键词
秸秆质外体蛋白
纤维素酶
纤维素酶活力
细胞壁蛋白
apoplast proteins of straw, cellulase, cellulase activity, cell wall bound proteins
