Production of Amylase in Liquid Culture by a Strain of
            <i>Aspergillus oryzae</i>

Kundu, Aditi; Das, Sumita

doi:10.1128/am.19.4.598-603.1970

Cited by 37 publications

(8 citation statements)

References 12 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…La actividad enzimática de la α-amilasa de Aspergillus oryzae a pH 5 no presenta una reducción mayor al 5% de actividad en el intervalo de temperatura de 40 -50°C en comparación con el intervalo 50 -60°C donde existe una pérdida del 30% de actividad, según los resultados descritos por Patel et al [15] y Kundu y Das [18].…”

Section: Resultados Y Discusionesunclassified

“…De acuerdo a los datos reportados por Patel et al [15] y Kundu -Das [18] para la α-amilasa de Aspergillus oryzae, el pH la actividad de la enzima es 5 a 50°C, que presenta una reducción del 4% de actividad cuando se reduce el pH a 4 y una reducción del 40% actividad a pH 3 para valores de pH ácidos, por el contrario en valores más básicos como pH 6 se observa una reducción del 20% de actividad, a pH 7 una reducción de 55% y a pH 10 no se presenta actividad enzimática.…”

Section: Resultados Y Discusionesunclassified

See 1 more Smart Citation

DETERMINACIÓN DE LOS PARAMETROS TEMPERATURA, pH Y CONCENTRACIÓN PARA LA NUEVA ENZIMA α-AMILASA Mg.

et al. 2019

View full text Add to dashboard Cite

Los parámetros fisicoquímicos de pH, concentración y temperatura de las reacciones de las α-amilasas en sus diferentes aplicaciones, determinan la eficiencia de la reacción enzimática. El presente estudio muestra la relación entre los parámetros fisicoquímicos demostrándose que el pH es el parámetro determinante para la eficiencia máxima de la enzima. También se determinan los valores óptimos de estos parámetros para la reacción enzimática a pH 5 y T=50°C para una concentración de 5,6 U/mL de la enzima, α-amilasa-Mg, modificada de acuerdo a la patente 002-2017.

show abstract

Section: Resultados Y Discusionesunclassified

DETERMINACIÓN DE LOS PARAMETROS TEMPERATURA, pH Y CONCENTRACIÓN PARA LA NUEVA ENZIMA α-AMILASA Mg.

et al. 2019

View full text Add to dashboard Cite

show abstract

“…The activation by Cu2+ ions is unique in the case of neutral proteinase of this strain. It is known that Cu2+ inhibits the enzyme activity of many enzymes (19,11,13,14,22). Recently it has been reported that Cu2+ activates the renin-like enzyme from Aspergil- a A 0.5-ml amount of enzyme solution, 0.2 ml of 10-1 M reagent, and 0.3 ml of glass distilled water were mixed together and kept at 30 C for 60 min.…”

Section: Discussionmentioning

confidence: 99%

Purification and Characterization of Extracellular Proteinases of Aspergillus oryzae

1983

Appl Environ Microbiol

View full text Add to dashboard Cite

The extracellular proteinases ofAspergillus oryzae EI 212 were separated into two active fractions by (NHJ)2SO4 and ethanol fractionation followed by diethylaminoethyl-Sephadex A-50 and hydroxyapatite chromatography. The molecular weight was estimated by gel filtration to be about 70,000 and 35,000 for proteinases I and II, respectively. Optimum pH for casein and hemoglobin hydrolysis was 6.5 at 60 C for proteinase I and 10.0 at 45 C for proteinase II, and for gelatin hydrolysis it was 6.5 at 45 C for both enzymes. The enzymes were stable over the pH range 6 to 8 at 30 C for 60 min. The enzyme activity for both the proteinases was accelerated by Cu2+ and inhibited by Fe2+, Fe3+, Hg2+, and Ag+. Halogenators (e.g., N-chlorosuccinimide) and diisopropyl fluorophosphate inhibited proteinase II. Sulfhydryl reagents such as p-chloromercuribenzoate and iodoacetate inhibited proteinase I. Sulfhydryl compounds accelerated the action of both enzymes.

show abstract

“…The enzyme α-amylase (EC 3.2.1.1 ) [27] breaks down long-chain saccharides (starch), yielding maltose, glucose, and "limit dextrin" from amylopectin (Equation 4).…”

Section: Equation-3mentioning

confidence: 99%

“…D2886) was tested on three DNA segments produced from the plasmid pZIP-mCMV-RFP-Puro-(V033), isolated from E.coli bacteria, and cut by three restriction enzymes: EcoRI-HF, BamHI-HF, and Nhel-HF. The DNA segments were incubated with a ligase T4 enzyme for 24h at 16 o C with ATP and a buffer, Tris-HCl (procedure described in [27]) in the presence of Cu 2+ and Cu + ions (1% CH3CN), under anaerobic conditions. The resulting DNA, separated by electrophoresis, and compared to the reaction mixture without the enzyme.…”

Section: Pcr (Polymerase Chain Reaction)mentioning

confidence: 99%

Monovalent Copper Ions Inhibit Enzymatic Systems

Saphier

Moshkovich

Popov

et al. 2021

Preprint

View full text Add to dashboard Cite

The effect of monovalent copper ions on enzymatic systems has hardly been studied to date; this is due to the low stability of monovalent copper ions in aqueous solutions, which led to the assumption that their concentration is negligible in biological systems. However, in an anaerobic atmosphere, and in the presence of a ligand that stabilizes the monovalent copper ions over the divalent copper ions, high and stable concentrations of monovalent copper ions can be reached. Moreover, the cell cytoplasm has a substantial concentration of potential stabilizers that can explain significant concentrations of monovalent copper ions in the cytoplasm. This study demonstrates the effect of monovalent and divalent copper ions on DNA polymerase, ligaseT4 DNA, the restriction enzymes EcoP15I and EcoR I, acid phosphatase, and α and βamylase enzymes. These systems were chosen because they can be monitored under conditions necessary for maintaining a stable concentration of monovalent copper ions, and since they exhibit a wide range of dependency on ATP. Previous studies indicated that ATP interacts with monovalent and divalent copper ions and stabilizing monovalent copper ions over divalent copper ions. The results showed that monovalent copper ions dramatically inhibit DNA polymerase and acid phosphatase, inhibit ligaseT4 DNA and the restriction enzyme EcoP15I, moderately inhibit α and β amylase, and have no effect on the restriction enzyme EcoR I. From the results presented in this work, it can be concluded that the mechanism is not one of oxidative stress, even though monovalent copper ions generate reactive oxygen species (ROS). Molecular oxygen in the medium, which is supposed to increase the oxidative stress, impairs the inhibitory effect of monovalent and divalent copper ions, and the kinetics of the inhibition is not suitable for the ROS mechanism.ATP forms a complex with copper ions (di and monovalent ions, where the latter is more stable) in which the metal ion is bound both to the nitrogen base and to the oxygen charged on the phosphate groups, forming an unusually distorted complex. The results of this study indicate that these complexes have the ability to inhibit enzymatic systems that are dependent on ATP.This finding can provide an explanation for the strong antimicrobial activity of monovalent copper ions, suggesting that rapid and lethal metabolic damage is the main mechanism of monovalent copper ions’ antimicrobial effect.

show abstract

Production of Amylase in Liquid Culture by a Strain of Aspergillus oryzae

Cited by 37 publications

References 12 publications

DETERMINACIÓN DE LOS PARAMETROS TEMPERATURA, pH Y CONCENTRACIÓN PARA LA NUEVA ENZIMA α-AMILASA Mg.

DETERMINACIÓN DE LOS PARAMETROS TEMPERATURA, pH Y CONCENTRACIÓN PARA LA NUEVA ENZIMA α-AMILASA Mg.

Purification and Characterization of Extracellular Proteinases of Aspergillus oryzae

Monovalent Copper Ions Inhibit Enzymatic Systems

Contact Info

Product

Resources

About