Endo/exo-synergism of cellulases increases with substrate conversion.
Synergy between cellulolytic enzymes is important for their industrial utilization, and numerous studies have addressed the problem of how to optimize the composition of enzyme cocktails with respect to this. The degree of synergy (DS) may change with substrate conversion, and some studies have suggested a maximum in DS early in the process. Here, we systematically investigated interrelationships of DS and conversion in a model system covering a wide range of experimental conditions. The results did not reveal any correlation between DS and contact time, but when plotted against the degree of substrate conversion we saw a systematic increase in DS. We suggest that this is linked to a decreasing reactivity of the substrate. Hence, synergy became increasingly important as the recalcitrance of the remaining substrate grew. Such conversion dependent changes in DS appear to be important both in mechanistic studies and attempts to find industrial enzymes blends with optimal synergy. Biotechnol. Bioeng. 2017;114: 696-700. © 2016 Wiley Periodicals, Inc.
Research Unit for Functional Biomaterials, Department of Science and Environment, Roskilde University, INM, 1 Universitetsvej, Build. 28, DK-4000, Roskilde, Denmark.
Johan Pelck
JP
Olsen
Novozymes A/S, Bagvaerd, Denmark.
Kim
K
Borch
Research Unit for Functional Biomaterials, Department of Science and Environment, Roskilde University, INM, 1 Universitetsvej, Build. 28, DK-4000, Roskilde, Denmark.
Peter
P
Westh
D002480:Cellulase / Q000737:chemistry* / Q000378:metabolism*; D002482:Cellulose / Q000032:analysis / Q000378:metabolism*; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism*; D006868:Hydrolysis; D035901:Hypocrea / Q000201:enzymology; D007700:Kinetics
D005656:Fungal Proteins; D002482:Cellulose; D002480:Cellulase
Cel7A; Cel7B; cellobiohydrolase; endoglucanase; synergism; synergy