Title

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

This document is currently not available here.

Share

COinS