Literature DB >> 24430147

Purification of glucoamylase fromAspergillus terreus.

S Ali1, Z Hossain, S Mahmood, R Alam.   

Abstract

Glucoamylase from a rice bran culture ofAspergillus terreus was purified by chromatography on DEAE-cellulose and concanavatin A-Sepharose. A homogenous monomer resulted after SDS-PAGE electrophoresis. The enzyme was a glycoprotein, molecular weight, 86,000 with 7.5% (w/w) carbohydrate content.

Entities:  

Year:  1990        PMID： 24430147     DOI： 10.1007/BF01202129

Source DB:  PubMed          Journal:  World J Microbiol Biotechnol        ISSN： 0959-3993            Impact factor:   3.312


  4 in total

1.  PROTEIN-CARBOHYDRATE INTERACTION. II. INHIBITION STUDIES ON THE INTERACTION OF CONCANAVALIN A WITH POLYSACCHARIDES.

Authors:  I J GOLDSTEIN; C E HOLLERMAN; E E SMITH
Journal:  Biochemistry       Date:  1965-05       Impact factor: 3.162

2.  Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

Authors:  U K Laemmli
Journal:  Nature       Date:  1970-08-15       Impact factor: 49.962

3.  Purification and properties of a glucoamylase fraction from the culture filtrate of Rhizopus nodosus.

Authors:  N Muthukumaran; S C Dhar
Journal:  Ital J Biochem       Date:  1983 Jul-Aug

4.  Fungal glucoamylases.

Authors:  P Manjunath; B C Shenoy; M R Raghavendra Rao
Journal:  J Appl Biochem       Date:  1983 Aug-Oct
  4 in total
  1 in total

1.  Direct production of itaconic acid from liquefied corn starch by genetically engineered Aspergillus terreus.

Authors:  Xuenian Huang; Mei Chen; Xuefeng Lu; Yueming Li; Xia Li; Jian-Jun Li
Journal:  Microb Cell Fact       Date:  2014-08-17       Impact factor: 5.328
  1 in total

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