Purification, characterization, and application of a thermostable dextranase from Talaromyces pinophilus.

Dextranase can hydrolyze dextran to low-molecular-weight polysaccharides, which have important medical applications. In the study, dextranase-producing strains were screened from various soil sources. The strain H6 was identified as Talaromyces pinophilus by a standard ITS rDNA analysis. Crude dextranase was purified by ammonium sulfate fractionation and Sepharose 6B chromatography, which resulted in a 6.69-fold increase in the specific activity and an 11.27% recovery. The enzyme was 58 kDa, lower than most dextranase, with an optimum temperature of 45 °C and an optimum pH of 6.0, and identified as an endodextranase. It was steady over a pH range from 3.0 to 10.0 and had reasonable thermal stability. The dextranase activity was increased by urea, which enhanced its activity to 115.35% and was conducive to clinical dextran production. Therefore, T. pinophilus H6 dextranase could show its superiority in practical applications.