Isolation of a pure dextranase from Penicillium funiculosum.
A dextranase, produced by Penicillium funiculosum, was purified 1,000-fold to yield the enzyme which was demonstrated by gel electrophoresis and electrofocusing to be a homogeneous protein. The purification method included acetone partition, ammonium sulfate fractionation, gel filtration, iron defecation and precipitation, and diethylaminoethyl-cellulose chromatography. The pure enzyme was also obtained by preparative gel electrophoresis. Gel-permeation chromatography indicates a molecular weight of 41,000. An isoelectric pH of 4.6 was established by electrofocusing. A 1-mg amount of the enzyme hydrolyzes a dextran substrate to yield 27,000 isomaltose reducing units in 2 hr.
D011232:Chemical Precipitation; D002848:Chromatography, DEAE-Cellulose; D003911:Dextrans / Q000378:metabolism; D004589:Electrophoresis, Disc; D005782:Gels; D006863:Hydrogen-Ion Concentration; D006867:Hydrolases / Q000032:analysis / Q000302:isolation & purification*; D007525:Isoelectric Focusing; D008970:Molecular Weight; D010407:Penicillium / Q000201:enzymology*; D013057:Spectrum Analysis
D003911:Dextrans; D005782:Gels; D006867:Hydrolases