1997
DOI: 10.1002/(sici)1097-0290(19971220)56:6<650::aid-bit8>3.0.co;2-m
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Substrate reactivity as a function of the extent of reaction in the enzymatic hydrolysis of lignocellulose

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Cited by 79 publications
(45 citation statements)
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“…Several groups have undertaken "restart" experiments wherein a partial hydrolysis is conducted, cellulase is removed, and the hydrolysis rate is measured on addition of new enzyme. As summarized in Table 7, results from restart experiments have been used as a basis to both confirm (488,776) and reject (152,233,507) declining substrate reactivity as a primary factor responsible for the declining rate phenomenon. Gusakov et al (233) explain declining rates in terms of deactivation of substrate-bound cellulase and product inhibition.…”
Section: Rates Of Enzymatic Hydrolysismentioning
confidence: 95%
See 1 more Smart Citation
“…Several groups have undertaken "restart" experiments wherein a partial hydrolysis is conducted, cellulase is removed, and the hydrolysis rate is measured on addition of new enzyme. As summarized in Table 7, results from restart experiments have been used as a basis to both confirm (488,776) and reject (152,233,507) declining substrate reactivity as a primary factor responsible for the declining rate phenomenon. Gusakov et al (233) explain declining rates in terms of deactivation of substrate-bound cellulase and product inhibition.…”
Section: Rates Of Enzymatic Hydrolysismentioning
confidence: 95%
“…A near-universal feature of cellulose hydrolysis observed in many studies over several decades is that the rate declines sharply as the reaction proceeds (corresponding to increasing values of ) in a batch hydrolysis. Measurements of rate in conjunction with adsorbed enzyme (152,498,507) confirm that the phenomenon of declining rate with increasing conversion is observed on a specific (rate per adsorbed enzyme) as well as absolute basis. Enzyme inactivation due to thermal effects (91, 117, 219), formation of an inactive enzyme-substrate (lignin) complex (234,506,657), and inhibition by hydrolysis products (91,233,377) have been implicated as important factors underlying the decreasing-rate phenomenon.…”
Section: Rates Of Enzymatic Hydrolysismentioning
confidence: 99%
“…Restarting hydrolysis with fresh enzyme is an adequate experiment to measure the losses of substrate reactivity [35,[40][41][42]. It is still difficult to explain the decrease of the reaction rate vis a vis the evolution of morphological features of the substrate.…”
Section: Introductionmentioning
confidence: 92%
“…Moreover, the assumption of two kinds of cellulose present in substrate was contradicted by Ooshima et aI. (1991), Desai and Converse (1997), and Yang et al (2006). It was found that the reactivity of substrate did not change during hydrolysis.…”
Section: Cellulose Hydrolysismentioning
confidence: 99%
“…Moreover, this theory was contradicted by Ooshima et ai. (1991), Desai and Converse (1997), and Yang et al (2006), who all found that the reactivity of substrate changed little during hydrolysis. Also, the two-types of cellulose mechanism cannot explain the monophasic first-order reaction for some substrates such as cotton and regenerated cellulose (Lenz et aI., 1990;Schurz and Honel, 1989).…”
Section: Introductionmentioning
confidence: 99%