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Ruminant Nutrition and Forage Utilization
Asian-Australasian Journal of Animal Sciences 2006;19(5): 684-689.
https://doi.org/10.5713/ajas.2006.684    Published online March 29, 2006.
Effect of Tween 80 on Hydrolytic Activity and Substrate Accessibility of Carbohydrolase I (CBH I) from Trichoderma viride
Wanjae Kim, Yuko Gamo, Yahaya Mohammed Sani, Yimiti Wusiman, Satoru Ogawa, Shuichi Karita, Masakazu Goto*, Masakazu Goto*
Correspondence:  Masakazu Goto,
Masakazu Goto,
The present study examined the effects of Tween 80 on the attachment and hydrolytic activity of a cellulase enzyme against ball-milled cellulose (BMC), using the whole component (native CBH I) and the catalysis module (core CBH I) of carbohydrolase I purified from Trichoderma viride (Meicelase, Meiji Seika, Tokyo, Japan). The effects were evaluated as protein concentrations in the supernatant after mixing enzyme and substrate with Tween 80 at room temperature. Tween 80 decreased the adsorption of native CBH I and core CBH I onto BMC (p<0.001) and increased the amount of reducing sugars released from BMC by native CBH I (p<0.001). However, Tween 80 did not enhance the hydrolytic activity of core CBH I. Observations using SEM revealed that Tween 80 caused cellulose filter paper to swell and enhanced surface cracks and filaments caused by native CBH I but not by core CBH I. These results suggested that Tween 80 decreases enzyme adsorption to its substrate but enhances enzymatic activity.
Keywords: Enzymatic Activity; Cellobiohydrolase; Tween 80
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