Purification and characterization of two different alpha-L-rhamnosidases, RhaA and RhaB, from Aspergillus aculeatus
Article Abstract:
Two alpha-L-rhamnosidases from Aspergillus aculeatus are described. These enzymes are used in the food and beverage industry and Aspergillus aculeatus is a good source of pectinolytic enzymes.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2001
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Molecular cloning and expression in Saccharomyces cerevisiae of two Aspergillus nidulans xylanase genes
Article Abstract:
Saccharomyces cerevisiae cells expressing Aspergillus nidulans xlnA and xlnB genes produce X(sub 22) and X(sub 24) xylanases that hydrolyze xylan. The cells expressing xlnA show greater xylanase activity than those expressing xlnB. Xylanase activity in recombinant S. cerevisiae is less than that in A. nidulans cells transformed with the xlnA and xlnB genes and their upstream amino acids. The genes are open reading frames containing introns. The xlnA encoded protein has 187 residues and a molecular weight of 20,247 while the xlnB encoded protein has 182 residues and a molecular weight of 20,088.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1996
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Differential expression of three alpha-galactosidase genes and a single beta-galactosidase gene from Aspergillus niger
Article Abstract:
A gene encoding a third alpha-galactosidase (AglB) from Aspergillus niger has been cloned and sequenced. An alignment of AglB amino acid sequence with alpha-galatosidases revealed that it belongs to a family of alpha-galatosidases that also includes A. niger AglA. The expression of the genes aglA, aglB, aglC and lacA was studied using monomeric, oligomeric and polymeric compounds as growth substrates. All four genes have distinct expression patterns which seem to mirror the natural substrates of the encoded proteins.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1999
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