TMAOase, trimethylamine-N-oxide demethylase, isa thermostable and active enzyme at 80°C
Purified trimethylamine-N-oxide demethylase (TMAOase)from walleye pollack muscle is a thermostable protein that was notinactivated after heating at 80°C for 30 min.The heated enzyme was electrophoresed in the same manner as fornative enzyme. Circular dichroism (CD) spectra for purified enzymechanged reversibly in the temperature range of 10–80°C.As the enzyme was still active at 80°C, the CD spectralchange did not directly relate to enzyme activity. TMAOase activity inthe myofibrillar fraction decreased sharply above 30°C,but was extracted and recovered from the heated myofibrillar fraction,suggesting that the activity seemed to be interrupted and apparently inactivateddue to the thermal alteration of myofibrillar proteins or some unknownfactors. The complicated profile found in dimethylamine (DMA) formationfrom trimethylamine-N-oxide (TMAO) in walleye pollack muscleduring heating consisted of both enzymic and non-enzymic processes.Most DMA was produced enzymatically below 40°C and interruptedabove 40°C. Therefore, DMA and trimethylamine was formednon-enzymatically at high temperatures regardless of the presenceof native enzyme. A new, simple and easy purification method wasproposed based on the thermostable nature of the enzyme.
Document Type: Research Article
Affiliations: 1: Laboratory of Food Biochemistry,Graduate School of Fisheries Sciences, Hokkaido University, Hakodate,Hokkaido 041-8611 and 2: Central ResearchLaboratory, Nippon Suisan Kaisha Ltd, Hachioji, Tokyo 192-0906,Japan
Publication date: April 1, 2003