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    Biotechnol Biofuels. 2010 Mar 23;3:6.

    Comparison of mechanistic models in the initial rate enzymatic hydrolysis of AFEX-treated wheat straw.

    Source

    Mascoma Corporation, 67 Etna Road, Suite 300, Lebanon, NH 03766, USA.

    Abstract

    BACKGROUND:

    Different mechanistic models have been used in the literature to describe the enzymatic hydrolysis of pretreated biomass. Although these different models have been applied to different substrates, most of these mechanistic models fit into two- and three-parameter mechanistic models. The purpose of this study is to compare the models and determine the activation energy and the enthalpy of adsorption of Trichoderma reesei enzymes on ammonia fibre explosion (AFEX)-treated wheat straw. Experimental enzymatic hydrolysis data from AFEX-treated wheat straw were modelled with two- and three-parameter mechanistic models from the literature. In order to discriminate between the models, initial rate data at 49 degrees C were subjected to statistical analysis (analysis of variance and scatter plots).

    RESULTS:

    For three-parameter models, the HCH-1 model best fitted the experimental data; for two-parameter models Michaelis-Menten (M-M) best fitted the experimental data. All the three-parameter models fitted the data better than the two-parameter models. The best three models at 49 degrees C (HCH-1, Huang and M-M) were compared using initial rate data at three temperatures (35 degrees , 42 degrees and 49 degrees C). The HCH-1 model provided the best fit based on the F values, the scatter plot and the residual sum of squares. Also, its kinetic parameters were linear in Arrhenius/van't Hoff's plots, unlike the other models. The activation energy (Ea) is 47.6 kJ/mol and the enthalpy change of adsorption (DeltaH) is -118 kJ/mol for T. reesei enzymes on AFEX-treated wheat straw.

    CONCLUSION:

    Among the two-parameter models, Michaelis-Menten model provided the best fit compared to models proposed by Humphrey and Wald. For the three-parameter models, HCH-1 provided the best fit because the model includes a fractional coverage parameter (varphi) which accounts for the number of reactive sites covered by the enzymes.

    PMID:
    20331857
    [PubMed]
    PMCID: PMC2856543
    Free PMC Article

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