Characterization of D-galacturonate reductase purified from the psychrophilic yeast species Cryptococcus diffluens(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)

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D-Galacturonic acid reductase was purified from a psychrophilic yeast strain of Cryptococcus diffluens, which was isolated from Satho, a traditional alcohol drink in Thailand. This enzyme, named Cd-GalUAR, assimilates D-galacturonic acid and requires NADPH as a cofactor. Cd-GalUAR is about 45kDa and stable from pH 6.5 to 7.5 and up to 35℃. Its optimum pH and temperature are pH 7.0 and 40℃, respectively. However, 80% of its maximum activity remained at 4℃. The reaction of Cd-GalUAR from D-galacturonic acid produces L-galactonic acid, which was identified by ^<13>C NMR and LC-MS. Three amino acid sequences were determined from trypsin-digested peptides of Cd-GalUAR. Similar sequences are found in many NAD or NADP oxidoreductases, including some D-galacturonate reductases. Our results suggest that Cd-GalUAR is the first D-galacturonate reductase identified in yeast.