Identification, Characterization, And Partial Purification Of Glucoamylase From Aspergillus Niger (Syn A. Ficuum) Nrrl 3135

Abstract

The crude extracellular extract of Aspergillus niger (syn A.ficuum) NRRL 3135 contains glucoamylase (exo-l,4-α-D-glucanohydrolase, EC 3.2.1.2). The enzyme, a glycoprotein, was purified 7-fold by ion-exchange chromatography, chromatofocusing, and conconavalin A affinity chromatography. The molecular weight of the enzyme was estimated to be 90 kDa by SDS-PAGE and gel permeation chromatography. The pI of the enzyme was 3.4. The temperature optimum of the enzyme was 60°C and the pH optimum was 5.0. The Vmax values for soluble starch, maltose, maltotriose, maltotetraose, maltopentaose, and isomaltose were 55.2, 11.7, 32.3, 47.8, 59.2, 12.5 nKat glucose/sec, respectively and the Km values for the same substrates were 0.09%, 0.67 mM, 0.76 mM, 0.76 mM, 0.68 mM, and 122.01 mM, respectively. © 1995, Taylor & Francis Group, LLC. All rights reserved.

Publication Date

1-1-1995

Publication Title

Preparative Biochemistry

Volume

25

Issue

1-2

Number of Pages

29-55

Document Type

Article

Personal Identifier

scopus

DOI Link

https://doi.org/10.1080/10826069508010106

Socpus ID

0029240435 (Scopus)

Source API URL

https://api.elsevier.com/content/abstract/scopus_id/0029240435

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