Sg. Desai et Ao. Converse, SUBSTRATE REACTIVITY AS A FUNCTION OF THE EXTENT OF REACTION IN THE ENZYMATIC-HYDROLYSIS OF LIGNOCELLULOSE, Biotechnology and bioengineering, 56(6), 1997, pp. 650-655
In an effort to better understand the role of the substrate in the rap
id fall off in the rate of enzymatic hydrolysis of cellulose with conv
ersion, substrate reactivity was measured as a function of conversion.
These measurements were made by interrupting the hydrolysis of pretre
ated wood at various degrees of conversion; and, after boiling and was
hing, restarting the hydrolysis in fresh buffer with fresh enzyme, The
comparison of the restart rate per enzyme adsorbed with the initial r
ate per enzyme adsorbed, both extrapolated back to zero con version, p
rovides a measurement of the substrate reactivity without the complica
tions of product inhibition or cellulase inactivation. The results ind
icate that the substrate reactivity falls only modestly as conversion
in creases. However, the restart rate is still higher than the rate of
the uninterrupted hydrolysis, particularly at high conversion. Hence
we conclude that the loss of substrate reactivity is not the principal
cause for the long residence time required for complete conversion. (
C) 1997 John Wiley & Sons, Inc.