Applied Microbiology and Biotechnology

, Volume 98, Issue 10, pp 4409–4420

Investigating commercial cellulase performances toward specific biomass recalcitrance factors using reference substrates

  • Xiaohui Ju
  • Mark Bowden
  • Mark Engelhard
  • Xiao Zhang
Biotechnologically relevant enzymes and proteins

DOI: 10.1007/s00253-013-5450-4

Cite this article as:
Ju, X., Bowden, M., Engelhard, M. et al. Appl Microbiol Biotechnol (2014) 98: 4409. doi:10.1007/s00253-013-5450-4

Abstract

Three commercial cellulase preparations, Novozymes Cellic® Ctec2, Dupont Accellerase® 1500, and DSM Cytolase CL, were evaluated for their hydrolytic activity using a set of reference biomass substrates with controlled substrate characteristics. It was found that lignin remains a significant recalcitrance factor to all the preparations, although different enzyme preparations respond to the inhibitory effect of lignin differently. Also, different types of biomass lignin can inhibit cellulase enzymes in different manners. Enhancing enzyme activity toward biomass fiber swelling is an area significantly contributing to potential improvement in cellulase performance. While the degree of polymerization of cellulose in the reference substrates did not present a major recalcitrance factor to Novozymes Cellic® Ctec2, cellulose crystallite has been shown to have a significant lower reactivity toward all enzyme mixtures. The presence of polysaccharide monooxygenases (PMOs) in Novozymes Ctec2 appears to enhance enzyme activity toward decrystallization of cellulose. This study demonstrated that reference substrates with controlled chemical and physical characteristics of structural features can be applied as an effective and practical strategy to identify cellulosic enzyme activities toward specific biomass recalcitrance factor(s) and provide specific targets for enzyme improvement.

Keywords

CellulaseHydrolytic efficiencyReference substratesLigninNanocrystalline cellulosePMOs

Supplementary material

253_2013_5450_MOESM1_ESM.pdf (267 kb)
ESM 1(PDF 266 kb)

Copyright information

© Springer-Verlag Berlin Heidelberg 2013

Authors and Affiliations

  • Xiaohui Ju
    • 1
  • Mark Bowden
    • 2
  • Mark Engelhard
    • 2
  • Xiao Zhang
    • 1
  1. 1.Voiland School of Chemical Engineering and Bioengineering, Bioproducts, Science and Engineering LaboratoryWashington State UniversityRichlandUSA
  2. 2.Environmental Molecular Science Laboratory, Pacific Northwest National LaboratoryRichlandUSA