JGC Corporation, 2205, Narita-cho, Oarai-machi, Higashiibaraki-gun, Ibaraki Pref. 311-1313, Japan.
Bioresour Technol. 2013 Aug;142:535-9. doi: 10.1016/j.biortech.2013.05.078. Epub 2013 May 27.
The mechanism of the increase in the hydrolysis rate and yield by the addition of Tween 80 to the hydrolysis reaction of filter paper was investigated under static and agitated conditions. The increase in the hydrolysis rate by addition of Tween 80 was observed under the agitated condition only. The effects of Tween 80 on the changes in the protein concentration of individual cellulase components were investigated in the absence of substrates. Agitation of the enzyme solution resulted in the drastic decrease of SDS-PAGE bands intensity of CBH2 (cellobiohydrolase 2). The addition of Tween 80 prevented this. Thus, the Tween 80 functions to stabilize instable cellulase components under the agitated condition. Moreover, addition of Tween 80 completely suppressed the decrease of CBH2 intensity by agitation at 30°C. Results suggest that Tween 80 stabilizes instable cellulase components not only during hydrolysis, but during enzyme production also.
在静态和搅拌条件下研究了吐温 80 对滤纸水解反应水解速率和产率增加的作用机制。仅在搅拌条件下观察到添加吐温 80 可提高水解速率。在没有底物的情况下，研究了吐温 80 对个别纤维素酶组分蛋白浓度变化的影响。酶溶液的搅拌导致 CBH2（纤维二糖水解酶 2）的 SDS-PAGE 带强度急剧下降。添加吐温 80 可防止这种情况发生。因此，吐温 80 的作用是在搅拌条件下稳定不稳定的纤维素酶成分。此外，添加吐温 80 可完全抑制在 30°C 搅拌时 CBH2 强度的降低。结果表明，吐温 80 不仅在水解过程中，而且在酶生产过程中也能稳定不稳定的纤维素酶成分。
