BACKGROUND: Cellulase is an enzyme of the glycosyl hydrolase family that catalyses the cleavage of β-1,4 glycosidic bonds in cellulose. In this study an alternating magnetic field was applied to evaluate cellulase activity using carboxymethyl cellulose (CMC) as substrate. RESULTS: The maximum and minimum activities of cellulase occurred when magnetic fields of 2.2 and 4.2 mT respectively were applied for 20 min. Following these treatments, the enzymatic parameters K(m) and V(m) were determined based on fitting to the Michaelis-Menten equations. Generally, K(m) showed the opposite trend to V(m) under magnetic field treatments. Treatment of enzyme/substrate solutions at 4.2 mT inhibited enzyme activity whereas treatment at 2.2 mT promoted it. CONCLUSION: It appears that treating enzyme/substrate solutions with different magnetic fields can inhibit or promote enzyme activity. Further research is needed to determine how the magnetic field influences the enzyme and substrate.
BACKGROUND: Cellulase is an enzyme of the glycosyl hydrolase family that catalyses the cleavage of β-1,4 glycosidic bonds in cellulose. In this study an alternating magnetic field was applied to evaluate cellulase activity using carboxymethyl cellulose (CMC) as substrate. RESULTS: The maximum and minimum activities of cellulase occurred when magnetic fields of 2.2 and 4.2 mT respectively were applied for 20 min. Following these treatments, the enzymatic parameters K(m) and V(m) were determined based on fitting to the Michaelis-Menten equations. Generally, K(m) showed the opposite trend to V(m) under magnetic field treatments. Treatment of enzyme/substrate solutions at 4.2 mT inhibited enzyme activity whereas treatment at 2.2 mT promoted it. CONCLUSION: It appears that treating enzyme/substrate solutions with different magnetic fields can inhibit or promote enzyme activity. Further research is needed to determine how the magnetic field influences the enzyme and substrate.