Characterization of Cold- and High-Pressure-Active Polygalacturonases from a Deep-Sea Yeast, Cryptococcus liquefaciens Strain N6
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A deep-sea yeast, <I>Cryptococcus liquefaciens</I> strain N6, produces two polygalacturonases, p36 and p40 (N6-PGases). These N6-PGases were highly active at 0–10 °C in comparison to a PGase from <I>Aspergillus japonicus</I>. The hydrolytic activity of these N6-PGases remained almost unchanged up to a hydrostatic pressure of 100 MPa at 24 °C with a very small activation volume of −1.1 ml/mol. At 10 °C, however, the activation volume increased to 3.3 or 5.4 ml/mol (p36 and p40, respectively), suggesting that the enzyme–substrate complexes can expand at their transition states. We speculate that such a volume expansion upon forming the enzyme–substrate complexes contributes to decreasing the activation energy for hydrolysis. This can account for the high activity of N6-PGases at low-temperature.
- Agricultural and Biological Chemistry
Agricultural and Biological Chemistry 70(1), 296-299, 2006-01-23
Japan Society for Bioscience, Biotechnology, and Agrochemistry