Enzyme kinetics study for heterogeneous system of pretreated kenaf hydrolysis

Abstract

The peculiarity of spatially restricted diffusion and molecular collision processes results in considerable contrast in a reaction between the reactant and catalyst in the heterogeneous system from its corresponding homogeneous structure. The identification of the enzymatic hydrolysis process of pre-treated kenaf and to convert it into simple sugars employing a systematic kinetic investigation is the aims of this study. The influence of substrate concentration on xylanase hydrolysis was performed in water bath shakers. In-house recombinant xylanase expressed in Pichia pastoris was used for the hydrolysis at pH 4.0 in 50 mM sodium citrate buffer with 200 rpm agitation. Modified Prout-Tompkins equation was used for the heterogeneous substrate hydrolysis. The results obtained show that temperature simultaneously influenced the time dependency of the reducing sugar yield. Dependence of the enzymatic rate of reaction can be calculated effectively on the conversion of substrates over different temperatures. The activation energy needed for pretreated kenaf hydrolysis was among the least compared to other lignocelluloses, which was only 25.15 kJ/mol. In conclusion, the exponential kinetic equation by the Modified Prout-Tompkins equation offers a solid understanding of xylanase hydrolysis on the pretreated kenaf. Thus, the prediction of the degree of hydrolysis required at the predetermined temperature and time values used can be quickly and precisely determined.