Synergistic interaction of an endo-β-1,4-glucanase and a β-glucohydrolase leads to more efficient hydrolysis of cellulose-like polymers in the gecarcinid land crab, Gecarcoidea natalis
Benjamin J. Allardyce A B and Stuart M. Linton AA School of Life and Environmental Sciences, Deakin University, 75 Pigdons Road, Geelong, Vic. 3216, Australia.
B Corresponding author. Email: ben.allardyce@deakin.edu.au
Australian Journal of Zoology 60(5) 299-302 https://doi.org/10.1071/ZO12074
Submitted: 3 August 2012 Accepted: 8 January 2013 Published: 6 February 2013
Abstract
This study investigated synergism between endo-β-1,4-glucanase and β-glucohydrolase enzymes from Gecarcoidea natalis. Together, these enzymes efficiently hydrolyse the cellulose-like polymer, carboxymethyl cellulose, to glucose. Endo-β-1,4-glucanase and β-glucohydrolase, isolated previously from G. natalis, were incubated in vitro using a ratio of the measured activities that matches that found in their digestive juice (5.4 : 1). Their combined activity, measured as the release of glucose from carboxymethyl cellulose, was greater than the sum of their separate activities. Hence they synergistically released glucose from carboxymethyl cellulose (degree of synergy: 1.27). This may be due to the complementary nature of the products of endo-β-1,4-glucanase activity and the preferred substrates of the β-glucohydrolase. β-glucohydrolase may also enhance cellulose hydrolysis by removing cellobiose, a potential competitive inhibitor of endo-β-1,4-glucanase. The synergistic interaction of these two enzymes further supports the previous suggestion that this species possesses a novel two-enzyme cellulase system that differs from the traditional three-enzyme fungal model.
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