Enzymatic saccharification of acid pretreated corn stover Empirical and fractal kinetic modelling
Enzymatic hydrolysis of corn stover was studied at agitation speeds from 50 to 500 rpm in a stirred tank bioreactor, at high solid concentrations (20% w/w dry solid/suspension), 50 °C and 15.5 mgprotein·gglucane −1. Two empirical kinetic models have been fitted to empirical data, namely a potential model and a fractal one. For the former case, the global order dramatically decreases from 13 to 2 as agitation speed increases, suggesting an increment in the access of enzymes to cellulose in terms of chemisorption followed by hydrolysis. For its part, the fractal kinetic model fits better to data, showing its kinetic constant a constant augmentation with increasing agitation speed up to a constant value at 250 rpm and above, when mass transfer limitations are overcome. In contrast, the fractal exponent decreases with rising agitation speed till circa 0.19, suggesting higher accessibility of enzymes to the substrate. © 2016 Elsevier Ltd
| Main Authors: | , , , , |
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| Format: | journal article biblioteca |
| Language: | eng |
| Published: |
2016
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| Online Access: | http://hdl.handle.net/20.500.12792/5562 |
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| Summary: | Enzymatic hydrolysis of corn stover was studied at agitation speeds from 50 to 500 rpm in a stirred tank bioreactor, at high solid concentrations (20% w/w dry solid/suspension), 50 °C and 15.5 mgprotein·gglucane −1. Two empirical kinetic models have been fitted to empirical data, namely a potential model and a fractal one. For the former case, the global order dramatically decreases from 13 to 2 as agitation speed increases, suggesting an increment in the access of enzymes to cellulose in terms of chemisorption followed by hydrolysis. For its part, the fractal kinetic model fits better to data, showing its kinetic constant a constant augmentation with increasing agitation speed up to a constant value at 250 rpm and above, when mass transfer limitations are overcome. In contrast, the fractal exponent decreases with rising agitation speed till circa 0.19, suggesting higher accessibility of enzymes to the substrate. © 2016 Elsevier Ltd |
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