作者: YeJun Han , HongZhang Chen
DOI: 10.1016/J.ENZMICTEC.2007.05.012
关键词:
摘要: Abstract A cellulase synergistic protein named Zea h was purified from fresh postharvest corn stover through sequential treatments. The homogeneous by PAGE and SDS-PAGE examination, indicating its purity molecular weight ( M w ) of approximately 55.78 kDa. Comparing with (0.042 FPU) applied alone in hydrolysis filter paper, when (6 μg) were together, the rate increased a factor 2 within 1 h, total cellulose conversion 3 during 24 h's hydrolysis. Thermal stability analysis revealed that 50.2% synergetic activity recovered incubated water for 30 min at 100 °C, yet deactivated high pressure steam (160 °C) 5 min. Studies on mechanisms synergism between showed that, could increase adsorption onto substrate, decrease hydrogen-bond intensity CrI substrate. Yet has no activity, little effect under conditions It be concluded may modify structure paper weakening or rupturing hydrogen bonds, more it accessible to cellulase. unique property provides an opportunity decreasing enzyme loading while retaining same degree