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. 1970 Sep;20(3):421–426. doi: 10.1128/am.20.3.421-426.1970

Isolation of a Pure Dextranase from Penicillium funiculosum

L Chaiet 1, A J Kempf 1, R Harman 1, E Kaczka 1, R Weston 1, K Nollstadt 1, F J Wolf 1
PMCID: PMC376951  PMID: 5485722

Abstract

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.

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Selected References

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  1. Brownstone A. D. A versatile system for preparative electrophoresis in acrylamide gel. Anal Biochem. 1969 Jan;27(1):25–46. doi: 10.1016/0003-2697(69)90216-4. [DOI] [PubMed] [Google Scholar]
  2. Fitzgerald R. J., Spinell D. M., Stoudt T. H. Enzymatic removal of artificial plaques. Arch Oral Biol. 1968 Jan;13(1):125–128. doi: 10.1016/0003-9969(68)90042-3. [DOI] [PubMed] [Google Scholar]
  3. Jakoby W. B. A technique for the crystallization of proteins. Anal Biochem. 1968 Nov;26(2):295–298. doi: 10.1016/0003-2697(68)90340-0. [DOI] [PubMed] [Google Scholar]
  4. ORNSTEIN L. DISC ELECTROPHORESIS. I. BACKGROUND AND THEORY. Ann N Y Acad Sci. 1964 Dec 28;121:321–349. doi: 10.1111/j.1749-6632.1964.tb14207.x. [DOI] [PubMed] [Google Scholar]
  5. Susor W. A., Kochman M., Rutter W. J. Heterogeneity of presumably homogeneous protein preparations. Science. 1969 Sep 19;165(3899):1260–1262. doi: 10.1126/science.165.3899.1260. [DOI] [PubMed] [Google Scholar]
  6. TSUCHIYA H. M., JEANES A., BRICKER H. M., WILHAM C. A. Dextran-degrading enzymes from molds. J Bacteriol. 1952 Oct;64(4):513–519. doi: 10.1128/jb.64.4.513-519.1952. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Vesterberg O., Svensson H. Isoelectric fractionation, analysis, and characterization of ampholytes in natural pH gradients. IV. Further studies on the resolving power in connection with separation of myoglobins. Acta Chem Scand. 1966;20(3):820–834. doi: 10.3891/acta.chem.scand.20-0820. [DOI] [PubMed] [Google Scholar]
  8. WHEATON R. M., BAUMAN W. C. Nonionic separations with ion exchange resins. Ann N Y Acad Sci. 1953 Nov 11;57(3):159–176. doi: 10.1111/j.1749-6632.1953.tb36394.x. [DOI] [PubMed] [Google Scholar]

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