scholarly journals Production performances and antioxidant activities of laying hens fed Aspergillus oryzae and phytase co-fermented wheat bran

2020 ◽  
Author(s):  
Chung Ming Huang ◽  
Wen Yang Chuang ◽  
Wei Chih Lin ◽  
Li Jun Lin ◽  
Shang Chang Chang ◽  
...  
Keyword(s):  
Aspergillus Oryzae ◽  
Wheat Bran ◽  
Laying Hens ◽  
Antioxidant Activities

scholarly journals Distribution of Phenolic Acids and Antioxidant Activities of Different Bran Fractions from Three Pigmented Wheat Varieties

2018 ◽  
Vol 2018 ◽  
pp. 1-9 ◽  
Author(s):  
Jinli Zhang ◽  
Yan Ding ◽  
Haizhou Dong ◽  
Hanxue Hou ◽  
Xiansheng Zhang
Keyword(s):  
Phenolic Acids ◽  
Wheat Bran ◽  
Phenolic Acid ◽  
Phenolic Content ◽  
Antioxidant Activities ◽  
Radical Scavenging Activity ◽  
Radical Scavenging ◽  
Total Phenolic ◽  
Scavenging Activity ◽  
Wheat Varieties

Phenolic acid profiles and antioxidant activities of outer bran, coarse bran, and shorts from blue, black, and purple wheat were analyzed. Phenolic acids were mainly in the bound form in pigmented wheat bran fractions. Phenolic acid content decreased in the order of outer bran, coarse bran, and shorts for the three pigmented wheat varieties. HPLC analysis of phenolic extracts demonstrated that the bound form of phenolic acids contained more ferulic, isoferulic, and p-coumaric acids compared to their free counterparts. Among the three pigmented wheat varieties, the bran fractions from blue wheat contained higher bound phenolic acids than the other two pigmented wheat bran fractions, except for purple coarse bran. The blue wheat outer bran had the highest total bound phenolic acid of 3458.71 μg/g while the purple wheat shorts had the lowest of 1730.71 μg/g. The contribution of bound phenolic acids to the total phenolic content and antioxidant activity was significantly higher than that of free phenolic acids. Blue wheat bran fractions had the highest radical scavenging activity against DPPH∙ while those of purple wheat gained the highest ABTS∙+ scavenging activity. High correlations were observed between TPC and radical scavenging capacities for DPPH and ABTS (R2>0.85, P<0.05).

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.

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 Protease from Aspergillus oryzae: Biochemical Characterization and Application as a Potential Biocatalyst for Production of Protein Hydrolysates with Antioxidant Activities

2014 ◽  
Vol 2014 ◽  
pp. 1-11 ◽  
Author(s):  
Ruann Janser Soares de Castro ◽  
Helia Harumi Sato
Keyword(s):  
Aspergillus Oryzae ◽  
Biochemical Characterization ◽  
Antioxidant Activities ◽  
Soy Protein Isolate ◽  
Antioxidant Properties ◽  
Protein Isolate ◽  
Protein Hydrolysates ◽  
Optimum Temperature ◽  
Temperature Range ◽  
Ph Range

This study reports the biochemical characterization of a protease from Aspergillus oryzae LBA 01 and the study of the antioxidant properties of protein hydrolysates produced with this protease. The biochemical characterization showed that the enzyme was most active over the pH range 5.0–5.5 and was stable from pH 4.5 to 5.5. The optimum temperature range for activity was 55–60°C, and the enzyme was stable at temperatures below 45°C. The activation energy (Ea) for azocasein hydrolysis and temperature quotient (Q10) were found to be 37.98 kJ mol−1 and 1.64–1.53 at temperature range from 30 to 55°C, respectively. The enzyme exhibited t1/2 of 97.63 min and a D value of 324.31 at the optimum temperature for activity (57.2°C). Protease from A. oryzae LBA 01 was shown as a potentially useful biocatalyst for protein hydrolysis, increasing the antioxidant activities of soy protein isolate, bovine whey protein, and egg white protein from 2.0- to 10.0-fold.

Antihypertensive and antioxidant activities of enzymatic wheat bran protein hydrolysates

2019 ◽  
Vol 44 (1) ◽  
Author(s):  
Zhipeng Zou ◽  
Mingjie Wang ◽  
Zhigao Wang ◽  
Rotimi E. Aluko ◽  
Rong He
Keyword(s):  
Wheat Bran ◽  
Antioxidant Activities ◽  
Protein Hydrolysates

scholarly journals Effect of Different Combinations of Soybean and Wheat Bran on Enzyme Production from Aspergillus oryzae S

2012 ◽  
Vol 2 ◽  
pp. 68-72 ◽  
Author(s):  
Chuenjit Chancharoonpong ◽  
Pao-Chuan Hsieh ◽  
Shyang-Chwen Sheu
Keyword(s):  
Aspergillus Oryzae ◽  
Wheat Bran ◽  
Enzyme Production

scholarly journals Effect of Replacement of Wheat Bran or Defatted Rice Bran by Dried Poultry Waste in diets for Laying Hens

1975 ◽  
Vol 12 (3) ◽  
pp. 141-145
Author(s):  
Isao UMEDA ◽  
Hiroyuki MEKADA ◽  
Syoji EBISAWA ◽  
Kikuo FUTAMURA
Keyword(s):  
Rice Bran ◽  
Wheat Bran ◽  
Laying Hens ◽  
Poultry Waste ◽  
Defatted Rice Bran

scholarly journals Production of alkaline protease from Aspergillus oryzae isolated from seashore of Bay of Bengal

2018 ◽  
Vol 10 (4) ◽  
pp. 1210-1215 ◽  
Author(s):  
Raghu Ram M ◽  
Suman Kumar Yepuru
Keyword(s):  
Aspergillus Oryzae ◽  
Wheat Bran ◽  
Bay Of Bengal ◽  
Alkaline Protease ◽  
Protease Activity ◽  
Skim Milk ◽  
Protease Production ◽  
Chemical Parameters ◽  
Oil Cakes ◽  
Physical And Chemical

Aspergillus oryzae isolatedon  Potato dextrose agar  from soil samples of kottakoduru seashore of Bay of Bengal, Andhra Pradesh, India seashore of Bay of Bengal by spread plate method and was screened for alkaline protease production on Skim milk containing agar plates and identified by clear zones of protein hydrolysis around colonies. Different physical and chemical parameters such as pH, temperature, substrate concentration and incubation time were optimized for the better production of alkaline protease. The maximum protease activity was found at pH of 8 containing 10% wheat bran at 300C, after 72 hours of fermentation.ZnSO4was effective activator for protease activity and sodium dsulphate had shownmore than 50% inhibition of enzyme activity. Among the different oil cakes used for the production of enzyme the Sesame  oil cake proved to be suitable substrate after wheat bran for the production of protease by Aspergillus oryzae.

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