Results 181 to 190 of about 9,014 (216)

Immobilization of Glucoamylase on Cellulose

Starch - Stärke, 1988
AbstractThe effectiveness of immobilization of glucoamylase on cotton linters and beech wood pulp activated in a number of manners was examined as well as the kinetic properties of immobilized enzyme.
M. Przybyt, H. Sugier
openaire   +1 more source

Fungal glucoamylases.

Journal of applied biochemistry, 1984
Glucoamylase (alpha-1,4-glucan glucohydrolase, EC 3.2.1.3) from fungal sources is one of the microbial glycoproteins that has received considerable attention particularly because it is used in the commercial production of dextrose. Several investigators have isolated glucoamylase from various fungal sources.
P, Manjunath, B C, Shenoy, M R, Raghavendra Rao   +2 more
openaire   +1 more source

Effect of organic solvents on the activity of glucoamylase

Biotechnology and Bioengineering, 1986
AbstractHydrolyses of maltose, maltotriose, and soluble starch catalyzed by glucoamylase (Asp. Niger) were carried out in the aqueous solutions of methanol, ethanol, ethylene glycol, and 1,4‐dioxane at 40°C and at the optimum pH in the respective solutions.
H, Nagamoto, T, Yasuda, H, Inoue
openaire   +2 more sources

Glucoamylase Research: An Overview

Starch - Stärke, 1995
AbstractThis paper reviews the main features of glucoamylase research describing essentially more recent developments on microorganisms, production and properties of glucoamylases. It is an important industrial enzyme and is widely used in starch saccharification, brewing and distilling industry.
openaire   +1 more source

The Properties of Glucoamylase Soluble and Immobilized on DEAE‐Cellulose. Part II. Thermostability of Glucoamylase

Starch - Stärke, 1988
AbstractThe stability of glucoamylase as a catalyst of starch hydrolysis reaction against heat denaturation was examined for enzyme adsorbed on DEAE‐cellulose as well as in solution. The protective action of the substrate against inactivation of enzyme and the influence of the amount of enzyme adsorbed on its stability was studied.
M. Przybyt, H. Sugier
openaire   +1 more source

Two forms of the glucoamylase of Aspergillus niger

Archives of Biochemistry and Biophysics, 1969
Abstract Two forms of the glucoamylase (α-1,4-glucan glucohydrolase, E.C.3.2.1.3) of Asgillus niger have been purified by chromatography on DEAE-cellulose ion-exchange columns. The purified enzymes possessed a high degree of purity as indicated by paper electrophoresis, sedimentation velocity, and disc-gel electrophoresis.
D R, Lineback, I J, Russell, C, Rasmussen   +2 more
openaire   +2 more sources

Immobilized glucoamylase: A biocatalyst of dextrin hydrolysis

Applied Biochemistry and Microbiology, 2006
Heterogeneous biocatalysts of starch conversion based on glucoamylase and carbon-containing carriers were obtained, and their biocatalytic properties in enzymatic hydrolysis of corn dextrins were studied. It was shown that the morphology of the surface carbon layer of carriers markedly affected the properties of biocatalysts.
G A, Kovalenko, L V, Perminova, G V, Plaksin, T V, Chuenko, O V, Komova, N A, Rudina   +5 more
openaire   +2 more sources

[Isolation and sequencing of glucoamylase gene from a glucoamylase over producing strain].

Wei sheng wu xue bao = Acta microbiologica Sinica, 1994
Chromosomal DNA was isolated from the mycelia of Aspergillus niger T21, a strain producing glucoamylase at a high level. Southern blot analysis indicated that the glucoamylase gene is situated on a 2.5kb EcoR I -EcoR V fragment. Chromosomal DNA was digested completely with EcoR I, EcoR V.
L, Zhong, G, Tang, K, Yang
openaire   +1 more source

Mucosal glucoamylase activity

The Journal of Pediatrics, 1981
B, Kerzner, H R, Sloan
openaire   +2 more sources

Research progress of glucoamylase with industrial potential

Journal of Food Biochemistry, 2022
Xuyan Zong, Lei Wen, Yanting Wang
exaly