Cellulases, as environmentally appropriate catalysts specifically acting on cellulosic substrates, are important for the industrial conversion of lignocellulose and modification of cellulose products. The ability to processively act is a key for the complete enzymatic hydrolysis of naturally occurring, crystalline cellulose. EG1 is a glycoside hydrolase family 5 processive endoglucanase from<i> Volvariella volvacea </i>consisting of a carbohydrate binding module (CBM1) and a catalytic domain (CD). The processivity of EG1 on four cellulose substrates, filter Paper (FP), Avicel, the cotton linter pulp (CLP) and the needle bleached Kraft pulp (NBKP) was studied. The processivity of EG1 was represented by the percentage of soluble reducing sugars created from cellulose substrate account for total reducing sugars. The result showed that the processivity of EG1 on CLP was much higher than that of others. The interactions of EG1 with the four cellulose substrates were investigated by using thin films supported on quartz crystal microgravimetry (QCM). QCM-D date showed that the temperature and protein concentration affected the amount of adsorption of EG1 on the film. Although EG1 hydrolyzed CLP with the highest processivity, however its enzyme protein adsorption capacity was not higher than that of other three. The dissolving pulp which was refined by PFI, treated by EG1, then milled 20 times by disk grinding, followed by the high pressure homogenization at 0.5% of consistency in 600bar, for 40 times. The nanofibers with very good evenness can be prepared.

Processive action of glycoside hydrolase family 5 endoglucanase from v<i>olvariella volvacea </i>and its application in the preparation of nanofibers

2019 Spring National Meeting

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Processive action of glycoside hydrolase family 5 endoglucanase from volvariella volvacea and its application in the preparation of nanofibers