Dynamic changes of substrate reactivity and enzyme adsorption on partially hydrolyzed cellulose

Jian Shi, Dong Wu, Libing Zhang, Blake A. Simmons, Seema Singh, Bin Yang, Charles E. Wyman

Research output: Contribution to journalArticlepeer-review

21 Scopus citations


The enzymatic hydrolysis of cellulose is a thermodynamically challenging catalytic process that is influenced by both substrate-related and enzyme-related factors. In this study, a proteolysis approach was applied to recover and clean the partially converted cellulose at the different stages of enzymatic hydrolysis to monitor the hydrolysis rate as a function of substrate reactivity/accessibility and investigate surface characteristics of the partially converted cellulose. Enzyme-substrate interactions between individual key cellulase components from wild-type Trichoderma reesei and partially converted cellulose were followed and correlated to the enzyme adsorption capacity and dynamic sugar release. Results suggest that cellobiohydrolase CBH1 (Cel7A) and endoglucanases EG2 (Cel5A) adsorption capacities decreased as cellulose was progressively hydrolyzed, likely due to the “depletion” of binding sites. Furthermore, the degree of synergism between CBH1 and EG2 varied depending on the enzyme loading and the substrates. The results provide a better understanding of the relationship between dynamic change of substrate features and the functionality of various cellulase components during enzymatic hydrolysis. Biotechnol. Bioeng. 2017;114: 503–515.

Original languageEnglish
Pages (from-to)503-515
Number of pages13
JournalBiotechnology and Bioengineering
Issue number3
StatePublished - Mar 1 2017

Bibliographical note

Publisher Copyright:
© 2016 Wiley Periodicals, Inc.


  • cellulase
  • cellulose
  • enzyme–substrate interactions
  • proteolysis
  • reactivity

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology


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