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Zhou, X.H., Chen, H.Z. and Li, Z.H. (2004) CMCase activity assay as a method for cellulase adsorption analysis. Enzyme and Microbial Technology, 35, 455-459. doi:10.1016/j.enzmictec.2004.07.005

has been cited by the following article:

• TITLE: The activity and kinetic properties of cellulases in substrates containing metal ions and acid radicals

  AUTHORS: Ge Wang, Xiaowen Zhang, Li Wang, Keke Wang, Fanglin Peng, Linsong Wang

  KEYWORDS: Cellulase; Enzyme Activity; Enzyme Deactivation; Kinetics Parameters; Metal Ions; Anions

  JOURNAL NAME: Advances in Biological Chemistry, Vol.2 No.4, November 28, 2012

  ABSTRACT: The effects of various metal ions (Na+, K+, Ca2+, Mg2+, Al3+, Co2+) and anions (Cl–, SO2-4 and CH3COO–) on two cellulases were investigated. Fitting of the data to Michaelis-Menten kinetics showed that Al3+ noncom-petitively inhibited cellulase (Km = 22.68 g/L; Vmax = 0.269 mg/min at 5.0 mmol/L AlCl3) and Mg2+ competitively inhibited cellulase (Km = 50.0 g/L; Vmax = 0.434 mg/min at 10.0 mmol/L MgCl2) Different metal ions increased or decreased inhibition of cellulase activity slightly below 1 mmol/L and strongly over 10 mmol/L. The results indicated that filter paper activeity (FPA) was suitable for analysis of enzymatic saccharification with various lignocellulosic substrates whereas crude cellulase was suitable for applications in the biomass industry. Some metal ions were proved to inhibit cellulase reversibly.