PARTIAL PURIFICATION AND CHARACTERIZATION OF B-GALACTOSIDASE FROM ASPERGILLUS NIGER UV-5
Authors: not saved
Abstract:
The enzyme pgalactosidase from a mutant strain of A. niger UV-5 was partially purified using ammonium sulfate and acetone. The saturation range of 60-80% ammonium sulfate was found to yield 60.5% enzyme recovery with 2.4 fold purification. Acetone precipitation at enzyme: acetone ratio of 1 : 1.5 brought about a higher yield i.e. 68% and three-fold purification. The combined procedures of 1.5 volume solvent fractionation followed by 50% ammonium sulfate precipitation brought about 8-fold purification with 40% enzyme yield. The optimum temperature of the enzyme was 65°C and the optimum pH was 4- 5. The pgalactosidase was strongly inhibited by galactose. Comparative study of partially purified P-galactosidase in the present study with a commercial lactase from A. oryzae revealed comparable results
similar resources
partial purification and characterization of b-galactosidase from aspergillus niger uv-5
the enzyme pgalactosidase from a mutant strain of a. niger uv-5 was partially purified using ammonium sulfate and acetone. the saturation range of 60-80% ammonium sulfate was found to yield 60.5% enzyme recovery with 2.4 fold purification. acetone precipitation at enzyme: acetone ratio of 1 : 1.5 brought about a higher yield i.e. 68% and three-fold purification. the combined procedures of 1.5 v...
full textPurification and Zymography of lipase from Aspergillus niger PTCC5010
In this study, Aspergillus niger lipase after extraction of medium culture was precipitated with different percentages of acetone and purified by ion exchange chromatography using SP-sepharose HP and Q-sepharose HP. The process of purification of the anzyme was studied by electrophoresis and the molecular weight was detected and determined by Zymography using overlying containing phenol red and...
full textCloning, purification, and characterization of a heat- and alkaline-stable endoglucanase B from Aspergillus niger BCRC31494.
Endoglucanase B (EGLB) derived from Aspergillus niger BCRC31494 has been used in the food fermentation industry because of its thermal and alkaline tolerance. It was cloned and expressed in Pichia pastoris. According to sequence analysis, the gene open reading frame comprises 1,217 bp with five introns (GenBank GQ292753). According to sequence and protein domain analyses, EGLB was assigned to g...
full textDifferential expression of three alpha-galactosidase genes and a single beta-galactosidase gene from Aspergillus niger.
A gene encoding a third alpha-galactosidase (AglB) from Aspergillus niger has been cloned and sequenced. The gene consists of an open reading frame of 1,750 bp containing six introns. The gene encodes a protein of 443 amino acids which contains a eukaryotic signal sequence of 16 amino acids and seven putative N-glycosylation sites. The mature protein has a calculated molecular mass of 48,835 Da...
full textIsolation, purification and characterization of 5'-phosphodiesterase from Aspergillus fumigatus
5'-Phosphodiesterase (5'-PDE) catalyzes the hydrolysis of ribonucleic acid to obtain a mixture of ribonucleotides, such as 5'-guanosine monophosphate and 5'-adenosine monophosphate. In this study, a 5'-PDE was newly isolated and purified from Aspergillus fumigatus. Following purification, this enzyme exhibited a specific activity of 1036.76 U/mg protein, a molecular weight of 9.5 kDa, and an op...
full textPurification and properties of a cellulase from Aspergillus niger.
A cellulolytic enzyme was isolated from a commercial cellulase preparation form Aspergillus niger. A yield of about 50mg of enzyme was obtained per 100g of commerial cellulase. The isolated enzyme was homogeneous in the ultracentrifuge at pH 4.0 and 8.0, and in sodium dodecyl sulphate/polyacrylamide-gel electrophoresis but showed one major and two minor bands in disc gel electrophoresis. No car...
full textMy Resources
Journal title
volume 6 issue 1
pages -
publication date 1995-03-01
By following a journal you will be notified via email when a new issue of this journal is published.
Hosted on Doprax cloud platform doprax.com
copyright © 2015-2023