Cloning and Characterization of a Chitosanase Gene from the Koji Mold Aspergillus oryzae Strain IAM 2660

2001 ◽  
Vol 65 (4) ◽  
pp. 977-981 ◽  
Author(s):  
Xiao-Yong ZHANG ◽  
An-Lan DAI ◽  
Kouji KUROIWA ◽  
Ritsuko KODAIRA ◽  
Masahiro NOGAWA ◽  
...  
Keyword(s):  
Aspergillus Oryzae ◽  
Koji Mold

scholarly journals Disruption and Overexpression of Acid Phosphatase Gene (aphA) from a Miso Koji Mold, Aspergillus oryzae KBN630, and Characterization of the Gene Product

2012 ◽  
Vol 18 (1) ◽  
pp. 59-65 ◽  
Author(s):  
Shoko YOSHINO-YASUDA ◽  
Osamu HASEGAWA ◽  
Yoshimi IGA ◽  
Yohei SHIRAISHI ◽  
Yutaka WAGU ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Gene Product ◽  
Aspergillus Oryzae ◽  
Koji Mold ◽  
Acid Phosphatase Gene

scholarly journals Characterization of the Prolyl Dipeptidyl Peptidase Gene (dppIV) from the Koji Mold Aspergillus oryzae

1998 ◽  
Vol 64 (12) ◽  
pp. 4809-4815 ◽  
Author(s):  
Agnès Doumas ◽  
Peter van den Broek ◽  
Michael Affolter ◽  
Michel Monod
Keyword(s):  
Aspergillus Oryzae ◽  
Polypeptide Chain ◽  
Wheat Gluten ◽  
Methylotrophic Yeast ◽  
Dipeptidyl Peptidase ◽  
Culture Broth ◽  
Peptidase Activity ◽  
Koji Mold ◽  
Hydrolysis Of

ABSTRACT The koji mold Aspergillus oryzae secretes a prolyl dipeptidyl peptidase (DPPIV) when the fungus is cultivated in a medium containing wheat gluten as the sole nitrogen and carbon source (MMWG). We cloned and sequenced the DPPIV gene from an A. oryzae library by using the A. fumigatus dppIVgene as a probe. Reverse transcriptase PCR experiments showed that theA. oryzae dppIV gene consists of two exons, the first of which is only 6 bp long. The gene encodes an 87.2-kDa polypeptide chain which is secreted into the medium as a 95-kDa glycoprotein. Introduction of this gene into A. oryzae leads to overexpression of prolyl dipeptidyl peptidase activity, while disruption of the gene abolishes all prolyl dipeptidyl peptidase activity in MMWG. The dppIV null mutants did not exhibit any change in phenotype other than the absence of prolyl dipeptidyl peptidase activity, suggesting that this activity is not essential. This loss of activity diminished the number of dipeptides and increased the number of larger peptides present in the MMWG culture broth. These effects were reversed by the addition of purified, recombinant DPPIV from the methylotrophic yeast expression vector Pichia pastoris. Our results suggest that the DPPIV enzyme may be of importance in industrial hydrolysis of what gluten-based substrates, which are rich in Pro residues.

Overexpression and Characterization of an Extracellular Leucine Aminopeptidase from Aspergillus oryzae

2010 ◽  
Vol 62 (2) ◽  
pp. 557-564 ◽  
Author(s):  
Mayumi Matsushita-Morita ◽  
Sawaki Tada ◽  
Satoshi Suzuki ◽  
Ryota Hattori ◽  
Junichiro Marui ◽  
...  
Keyword(s):  
Aspergillus Oryzae ◽  
Leucine Aminopeptidase

Discovery of a new tyrosinase-like enzyme family lacking a C-terminally processed domain: production and characterization of an Aspergillus oryzae catechol oxidase

2009 ◽  
Vol 86 (1) ◽  
pp. 213-226 ◽  
Author(s):  
Chiara Gasparetti ◽  
Greta Faccio ◽  
Mikko Arvas ◽  
Johanna Buchert ◽  
Markku Saloheimo ◽  
...  
Keyword(s):  
Aspergillus Oryzae ◽  
Catechol Oxidase ◽  
Enzyme Family
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