scholarly journals Purification and Properties of Leucine Aminopeptidase I from Aspergillus oryzae

1973 ◽  
Vol 37 (4) ◽  
pp. 757-765 ◽  
Author(s):  
Tadanobu NAKADAI ◽  
Seiichi NASUNO ◽  
Nobuyoshi IGUCHI
Keyword(s):  
Aspergillus Oryzae ◽  
Leucine Aminopeptidase ◽  
Purification And Properties

scholarly journals Purification and Properties of Leucine Aminopeptidase II from Aspergillus oryzae

1973 ◽  
Vol 37 (4) ◽  
pp. 767-774 ◽  
Author(s):  
Tadanobu NAKADAI ◽  
Seiichi NASUNO ◽  
Nobuyoshi IGUCHI
Keyword(s):  
Aspergillus Oryzae ◽  
Leucine Aminopeptidase ◽  
Purification And Properties

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

scholarly journals Purification and Properties of Neutral Proteinase II from Aspergillus oryzae

1973 ◽  
Vol 37 (12) ◽  
pp. 2703-2708 ◽  
Author(s):  
Tadanobu NAKADAI ◽  
Seiichi NASUNO ◽  
Nobuyoshi IGUCHI
Keyword(s):  
Aspergillus Oryzae ◽  
Neutral Proteinase ◽  
Purification And Properties

Purification and properties of glutaminase from Aspergillus oryzae

1988 ◽  
Vol 66 (2) ◽  
pp. 137-143 ◽  
Author(s):  
Toshihiro Yano ◽  
Masae Ito ◽  
Kenji Tomita ◽  
Hidehiko Kumagai
Keyword(s):  
Aspergillus Oryzae ◽  
Purification And Properties

scholarly journals Aspergillus oryzae acid proteinase. Purification and properties, and formation of π-chymotrypsin

1975 ◽  
Vol 147 (1) ◽  
pp. 45-53 ◽  
Author(s):  
R Davidson ◽  
A Gertler ◽  
T Hofmann
Keyword(s):  
Aspergillus Oryzae ◽  
Deae Cellulose ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Molecular Forms ◽  
Acid Proteinase ◽  
Sedimentation Analysis ◽  
Simple Tool ◽  
Purification And Properties ◽  
Yield And Purity

An acid proteinase from Aspergillus oryzae was isolated from a commercial powder by successive (NH4)2SO4 fractionation, acetone precipitation, and ion-exchange chromatography on phosphate- and DEAE-cellulose columns. The purified enzyme was found to be homogeneous by ultracentrifuge-sedimentation analysis (S20, W equal 3.63S), but electrofocusing in polyacrylamide gels and electrophoresis at pH 3.2 revealed that it consists of two very closely migrating bands. No difference in the amino acid composition and enzymic activities of the two partially separated bands could be detected, and it was concluded that the acid proteinase exists in two molecular forms. The enzyme activates bovine trypsinogen and chymotrypsinogen at pH 3.5 (the kappacat. and Km values at 35degrees C are 11.3S- minus 1, 0.10mM and 1.14S- minus 1, 0.18mM respectively). It hydrolyses the Phe-Phe bond of the synthetic pepsin substrates Z-His-Phe-Phe-OEt (kappacat. equal 1.65S- minus 1, Km equal 0.640mM at pH 3.5, 30degrees C) and Z-Ala-Ala-Phe-Phe-OPy4Pr (kappacat. equal 0.37S- minus 1, Km equal 0.037 mM at pH2.9, 39degrees C), where Z represents benzyloxycarbonyl and OPy4Pr represents 3-(4-pyridyl)-propyl 1-ester. Activation of bovine chymotrypsinogen results from the cleavage of the Arg(15)-Ile(16) bond in the zymogen. No other cleavages were observed. The use of A. oryzae proteinase provides a simple tool for the production of pi-chymotrypsin in good yield and purity.

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