Further evidence on differentiation of Aspergillus sojae from Aspergillus oryzae by electrophoretic patterns of cellulase, pectin-lyase, and acid proteinase

1974 ◽  
Vol 20 (3) ◽  
pp. 413-416 ◽  
Author(s):  
S. Nasuno
Keyword(s):  
Aspergillus Oryzae ◽  
Wheat Bran ◽  
Pectin Lyase ◽  
Acid Proteinase ◽  
Solid Culture ◽  
Aspergillus Sojae ◽  
Electrophoretic Patterns ◽  
Cultural Conditions ◽  
Electrophoretic Mobilities ◽  
Species Specific

Cellulase (β-1,4-glucan-4-glucanohydrolase, EC. 3.2.1.4), pectin-lyase (EC. 4.2.2.3), and acid proteinase (aspergillopeptidase A) (EC. 3.4.4.17) extracted from wheat bran solid culture of 23 strains of Aspergillus oryzae and 21 strains of Aspergillus sojae showed species-specific patterns on electrophoresis in polyacrylamide gels. The electrophoretic patterns of the cellulase were independent of age or cultural conditions. The pectin-lyase patterns were also independent of culture age except early phase of growth. The species-specific patterns were clear at the stage of the maximum production of acid proteinase. With the exception of one strain, no variation of the electrophoretic mobilities of these key enzymes were observed between the strains of the same species. The results provide further evidence to support the establishment of A. sojae as a species distinct from A. oryzae and the use of the electrophoretic zymograms as a taxonomic aid.

scholarly journals Pectinase production by fungal strains in solid-state fermentation using agro-industrial bioproduct

2004 ◽  
Vol 47 (5) ◽  
pp. 813-819 ◽  
Author(s):  
Natalia Martin ◽  
Simone Regina de Souza ◽  
Roberto da Silva ◽  
Eleni Gomes
Keyword(s):  
Solid State ◽  
Wheat Bran ◽  
Solid State Fermentation ◽  
Sugar Cane Bagasse ◽  
Pectin Lyase ◽  
Optimum Activity ◽  
Fungal Strains ◽  
Penicillium Sp ◽  
Polygalacturonase Production ◽  
Pectinase Production

Pectin lyase and polygalacturonase production by newly isolated fungal strains was carried out in solid-state fermentation. Moniliella SB9 and Penicillium sp EGC5 produced polygalcturonase (PG) and pectin lyase (PL) on mixture of orange bagasse, sugar cane bagasse and wheat bran as substrate. PG and PL produced by Moniliella presented optimum activity at pH 4.5 and 10.0 and at 55 and 45°C, respectively, while these enzymes from Penicillium sp presented optimum activity at pH 4.5-5.0 and 9.0 and 40°C, respectively.

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.

scholarly journals Comparison of Volatile Components in Soy Sauce (Koikuchi Shoyu) Produced Using Aspergillus sojae and Aspergillus oryzae.

1996 ◽  
Vol 43 (9) ◽  
pp. 1063-1074 ◽  
Author(s):  
Kazuo ISHIHARA ◽  
Nobuo HONMA ◽  
Isao MATSUMOTO ◽  
Seiichi IMAI ◽  
Shinkichi NAKAZAWA ◽  
...  
Keyword(s):  
Aspergillus Oryzae ◽  
Soy Sauce ◽  
Volatile Components ◽  
Aspergillus Sojae

Identification and Toxigenic Potential of the Industrially Important Fungi, Aspergillus oryzae and Aspergillus sojae

2007 ◽  
Vol 70 (12) ◽  
pp. 2916-2934 ◽  
Author(s):  
THOMAS R. JØRGENSEN
Keyword(s):  
Aspergillus Oryzae ◽  
Aflatoxin Production ◽  
Molecular Evidence ◽  
Fermented Foods ◽  
Culture Collections ◽  
Aspergillus Sojae ◽  
Societal Issues ◽  
Traditional Preparation ◽  
Close Relatives ◽  
High Degree

Mold strains belonging to the species Aspergillus oryzae and Aspergillus sojae are highly valued as koji molds in the traditional preparation of fermented foods, such as miso, sake, and shoyu, and as protein production hosts in modern industrial processes. A. oryzae and A. sojae are relatives of the wild molds Aspergillus flavus and Aspergillus parasiticus. All four species are classified to the A. flavus group. Strains of the A. flavus group are characterized by a high degree of morphological similarity. Koji mold species are generally perceived of as being nontoxigenic, whereas wild molds are associated with the carcinogenic aflatoxins. Thus, reliable identification of individual strains is very important for application purposes. This review considers the pheno- and genotypic markers used in the classification of A. flavus group strains and specifically in the identification of A. oryzae and A. sojae strains. Separation of A. oryzae and A. sojae from A. flavus and A. parasiticus, respectively, is inconsistent, and both morphologic and molecular evidence support conspecificity. The high degree of identity is reflected by the divergent identification of reference cultures maintained in culture collections. As close relatives of aflatoxin-producing wild molds, koji molds possess an aflatoxin gene homolog cluster. Some strains identified as A. oryzae and A. sojae have been implicated in aflatoxin production. Identification of a strain as A. oryzae or A. sojae is no guarantee of its inability to produce aflatoxins or other toxic metabolites. Toxigenic potential must be determined specifically for individual strains. The species taxa, A. oryzae and A. sojae, are currently conserved by societal issues.

scholarly journals Influence of medium composition and pH on the production of polygalacturonases by Aspergillus oryzae

2004 ◽  
Vol 47 (5) ◽  
pp. 693-702 ◽  
Author(s):  
Eloane Malvessi ◽  
Mauricio Moura da Silveira
Keyword(s):  
Liquid Medium ◽  
Aspergillus Oryzae ◽  
Wheat Bran ◽  
Medium Composition ◽  
Citrus Fruits ◽  
A Value ◽  
Initial Ph ◽  
Normal Increase

A liquid medium containing wheat bran, salts and a source of inducer (pectin) was found to be suitable for the production of exo- and endo-polygalacturonases by Aspergillus oryzae CCT3940. Induction of polygalacturonases by purified pectin was significantly higher than when rinds of citrus fruits were used as inducer. A. oryzae growth was favoured by pH close to 4, although a drop of pH to around 3 was needed for enzymes production. Afterwards, decreasing activities were observed with the normal increase in pH to near neutrality. The highest activities were achieved with an initial pH of 4 and controlled when it decreased to a value slightly below 3 (159 units endo-PG.mL-1 at 83 h and 45 units exo-PG.mL-1 at 64 h), being the loss in polygalacturonases activities strongly reduced at this condition. The best values of pH and temperature for the action of exo-PG (4.5/57ºC) and endo-PG (4.3/40ºC) were assessed.

Sign in / Sign up

Export Citation Format

Share Document