Related Experiment Video
Updated: May 16, 2026

High-throughput Screening of Carbohydrate-degrading Enzymes Using Novel Insoluble Chromogenic Substrate Assay Kits
Published on: September 20, 2016
Enzymatic hydrolysis of microcrystalline cellulose and pretreated wheat straw: a detailed comparison using convenient
Mareike Monschein1, Christoph Reisinger, Bernd Nidetzky
1Austrian Center of Industrial Biotechnology GmbH, Petersgasse 14, 8010 Graz, Austria.
Abstract:
Marked slow-down of soluble sugar production at low degree of substrate conversion limits the space-time yield of enzymatic hydrolysis of ligno-cellulosic materials. A simple set of kinetic descriptors was developed to compare reducing sugar release from pure crystalline cellulose (Avicel) and pretreated wheat straw by Trichoderma reesei cellulase at 50 °C. The focus was on the rate-retarding effect of maximum hydrolysis rate at reaction start (r(max)), limiting hydrolysis rate (r(lim)) at extended reaction time (24h), and substrate conversion, marking the transition between the r(max) and r(lim) kinetic regimes (C(trans)). At apparent saturation of substrate (12.2g cellulose/L) with enzyme, r(max) for pretreated wheat straw (~9.6g/L/h) surpassed that for Avicel by about 1.7-fold whereas their r(lim) were almost identical (~0.15 g/L/h). C(trans) roughly doubled as enzyme/substrate loading was increased from 3.8 to 75FPU/g, suggesting C(trans) to be a complex manifestation of cellulase-cellulose interaction, not an intrinsic substrate property. A low-temperature adsorption step preceding hydrolysis at 50 °C resulted in enhanced cellulase binding at reaction start without increasing r(max). C(trans) was higher for pretreated wheat straw (~30%) than for Avicel (~20%) under these conditions.

