The Proteolytic Enzymes of Aspergillus oryzae. II. Properties of the Proteolytic Enzymes.

1963 ◽  
Vol 17 ◽  
pp. 1541-1551 ◽  
Author(s):  
Rolf Bergkvist ◽  
Anders Kjær ◽  
Bengt Lindberg ◽  
Hans Meier ◽  
Jon Munch-Petersen
Keyword(s):  
Aspergillus Oryzae ◽  
Proteolytic Enzymes

scholarly journals Canola Cake as a Potential Substrate for Proteolytic Enzymes Production by a Selected Strain of Aspergillus oryzae: Selection of Process Conditions and Product Characterization

2013 ◽  
Vol 2013 ◽  
pp. 1-8 ◽  
Author(s):  
Adriana C. Freitas ◽  
Ruann J. S. Castro ◽  
Maria A. Fontenele ◽  
Antonio S. Egito ◽  
Cristiane S. Farinas ◽  
...  
Keyword(s):  
Aspergillus Oryzae ◽  
Protease Activity ◽  
Incubation Temperature ◽  
Initial Conditions ◽  
Proteolytic Enzymes ◽  
Inoculum Size ◽  
Protease Production ◽  
Process Conditions ◽  
Enzymatic Extract ◽  
Technological Advances

Oil cakes have excellent nutritional value and offer considerable potential for use in biotechnological processes that employ solid-state fermentation (SSF) for the production of high value products. This work evaluates the feasibility of using canola cake as a substrate for protease production by a selected strain of Aspergillus oryzae cultivated under SSF. The influences of the following process parameters were considered: initial substrate moisture content, incubation temperature, inoculum size, and pH of the buffer used for protease extraction and activity analysis. Maximum protease activity was obtained after cultivating Aspergillus oryzae CCBP 001 at 20°C, using an inoculum size of 107 spores/g in canola cake medium moistened with 40 mL of water to 100 g of cake. Cultivation and extraction under selected conditions increased protease activity 5.8-fold, compared to the initial conditions. Zymogram analysis of the enzymatic extract showed that the protease molecular weights varied between 31 and 200 kDa. The concentrated protease extract induced clotting of casein in 5 min. The results demonstrate the potential application of canola cake for protease production under SSF and contribute to the technological advances needed to increase the efficiency of processes designed to add value to agroindustrial wastes.

scholarly journals Induction and Repression of Hydrolase Genes in Aspergillus oryzae

2021 ◽  
Vol 12 ◽  
Author(s):  
Mizuki Tanaka ◽  
Katsuya Gomi
Keyword(s):  
Gene Expression ◽  
Transcription Factor ◽  
Aspergillus Oryzae ◽  
Catabolite Repression ◽  
Food Industry ◽  
Carbon Catabolite Repression ◽  
Proteolytic Enzymes ◽  
Current Knowledge ◽  
Glycosyl Hydrolase ◽  
Fermented Foods

The filamentous fungus Aspergillus oryzae, also known as yellow koji mold, produces high levels of hydrolases such as amylolytic and proteolytic enzymes. This property of producing large amounts of hydrolases is one of the reasons why A. oryzae has been used in the production of traditional Japanese fermented foods and beverages. A wide variety of hydrolases produced by A. oryzae have been used in the food industry. The expression of hydrolase genes is induced by the presence of certain substrates, and various transcription factors that regulate such expression have been identified. In contrast, in the presence of glucose, the expression of the glycosyl hydrolase gene is generally repressed by carbon catabolite repression (CCR), which is mediated by the transcription factor CreA and ubiquitination/deubiquitination factors. In this review, we present the current knowledge on the regulation of hydrolase gene expression, including CCR, in A. oryzae.

scholarly journals The Proteolytic Enzymes of Aspergillus oryzae. I. Methods for the Estimation and Isolation of the Proteolytic Enzymes.

1963 ◽  
Vol 17 ◽  
pp. 1521-1540 ◽  
Author(s):  
Rolf Bergkvist ◽  
Anders Kjær ◽  
Bengt Lindberg ◽  
Hans Meier ◽  
Jon Munch-Petersen
Keyword(s):  
Aspergillus Oryzae ◽  
Proteolytic Enzymes

scholarly journals The Proteolytic Enzymes of Aspergillus oryzae. IV. On the Inhibition of the Enzymes by Serum.

1963 ◽  
Vol 17 ◽  
pp. 2239-2249 ◽  
Author(s):  
Rolf Bergkvist ◽  
P. Olesen Larsen ◽  
Salo Gronowitz ◽  
Birgitta Mathiasson ◽  
Jon Munch-Petersen
Keyword(s):  
Aspergillus Oryzae ◽  
Proteolytic Enzymes

scholarly journals The Proteolytic Enzymes of Aspergillus oryzae. III. A Comparison of the Fibrinolytic and Fibrinogenolytic Effects of the Enzymes.

1963 ◽  
Vol 17 ◽  
pp. 2230-2238 ◽  
Author(s):  
Rolf Bergkvist ◽  
P. Olesen Larsen ◽  
Salo Gronowitz ◽  
Birgitta Mathiasson ◽  
Jon Munch-Petersen
Keyword(s):  
Aspergillus Oryzae ◽  
Proteolytic Enzymes

The ubiquitin–proteasome system and skeletal muscle wasting

2005 ◽  
Vol 41 ◽  
pp. 173-186 ◽  
Author(s):  
Didier Attaix ◽  
Sophie Ventadour ◽  
Audrey Codran ◽  
Daniel Béchet ◽  
Daniel Taillandier ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Wasting ◽  
Proteolytic Enzymes ◽  
Cathepsin L ◽  
Ubiquitin Proteasome System ◽  
Complete Breakdown ◽  
Skeletal Muscle Proteins ◽  
Ubiquitin Proteasome ◽  
Tripeptidyl Peptidase Ii ◽  
F Box Protein

The ubiquitin–proteasome system (UPS) is believed to degrade the major contractile skeletal muscle proteins and plays a major role in muscle wasting. Different and multiple events in the ubiquitination, deubiquitination and proteolytic machineries are responsible for the activation of the system and subsequent muscle wasting. However, other proteolytic enzymes act upstream (possibly m-calpain, cathepsin L, and/or caspase 3) and downstream (tripeptidyl-peptidase II and aminopeptidases) of the UPS, for the complete breakdown of the myofibrillar proteins into free amino acids. Recent studies have identified a few critical proteins that seem necessary for muscle wasting {i.e. the MAFbx (muscle atrophy F-box protein, also called atrogin-1) and MuRF-1 [muscle-specific RING (really interesting new gene) finger 1] ubiquitin–protein ligases}. The characterization of their signalling pathways is leading to new pharmacological approaches that can be useful to block or partially prevent muscle wasting in human patients.

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