scholarly journals Kinetic properties of α-amylase produced by Bacillus megaterium RAS103 under optimum conditions in submerged fermentation

2018 ◽  
Vol 0 (0) ◽  
pp. 0-0
Author(s):  
Abdel-Hamied Rasmey
Keyword(s):  
Bacillus Megaterium ◽  
Submerged Fermentation ◽  
Kinetic Properties ◽  
Optimum Conditions

Biosynthesis of L-lysine by Bacillus megaterium through submerged fermentation

2020 ◽  
Vol 52 (6) ◽  
Author(s):  
Amjad Hussain ◽  
Hamid Mukhtar ◽  
Ikram Ul Haq
Keyword(s):  
Bacillus Megaterium ◽  
Submerged Fermentation

scholarly journals Preparation of Laccase Immobilized Cryogels and Usage for Decolorization

2013 ◽  
Vol 2013 ◽  
pp. 1-7 ◽  
Author(s):  
Murat Uygun
Keyword(s):  
Glycidyl Methacrylate ◽  
Kinetic Properties ◽  
Optimum Temperature ◽  
Optimum Conditions ◽  
Immobilized Laccase ◽  
Optimum Ph ◽  
Edx Analyses ◽  
Swelling Studies ◽  
Laccase Enzyme ◽  
Thermal Stability Of

Poly(methyl methacrylate-co-glycidyl methacrylate) (poly(MMA-co-GMA)) cryogels were synthesized by radical cryopolymerization technique. Then, laccase enzyme was covalently attached to the cryogel and characterized by using swelling studies and SEM and EDX analyses. Kinetic properties and optimum conditions of the immobilized and free laccase were studied and it was found that of the immobilized laccase was lower than that of free laccase. of the immobilized laccase was increased upon immobilization. Optimum pH was found to be 4.0 for each type of laccase, while optimum temperature was shifted to the warmer region after the immobilization. It was also found that thermal stability of the immobilized laccase was higher than that of free laccase. Immobilized laccase could be used for 10 times successive reuse with no significant decrease in its activity. Also, these laccase immobilized cryogels were successfully used for the decolorization of seven different dyes.

scholarly journals Improvement of Tannase Production from Bacillus Bacteria by Submerged Fermentation of Spent Tea

2021 ◽  
Author(s):  
Rasha Al Haddad ◽  
Mohamad Tahla ◽  
Lina Al Amir
Keyword(s):  
Gallic Acid ◽  
Submerged Fermentation ◽  
Rotation Speed ◽  
Animal Feed ◽  
Statistical Design ◽  
Oil Industry ◽  
Optimum Conditions ◽  
Genus Bacillus ◽  
Hydrolysis Of

Tannase is an enzyme that causes hydrolysis of a group of tannins (gallo-tannins) to gallic acid and glucose. This enzyme is of importance due to its numerous applications in many fields, such as in the food industry by enhancing tea and coffee flavor and improving the quality of fruit juices rich in tannins. Tannase is also of importance in improving the quality of animal feed. Gallic acid is applied in the drug industry, and the production of antioxidants is used in the oil industry. This study was carried out to improve production of tannase from genus Bacillus using spent tea as a substrate by submerged fermentation and applying the statistical design Response Surface Methodology (RSM). Five parameters were considered, and each parameter was studied at five levels. They were temperature range (25 to 45˚C), pH (3–8), incubation period (24–120 hours), spent tea (0.5–2.5%) and rotation speed (100–300rpm). Results obtained revealed that optimum conditions for maximum production of tannase were: temperature at 35˚C, pH at 5, incubation time of 48 hours, spent tea concentration 1.5%, and rotation speed of 150 rpm. We recommend that further studies be carried out to clarify and determine the properties of crude and purified enzymes.

Alkaline phosphatase of high and low molecular mass in human serum and bile: a comparative study of kinetic properties.

1980 ◽  
Vol 26 (3) ◽  
pp. 451-456
Author(s):  
P M Crofton ◽  
A F Smith
Keyword(s):  
Alkaline Phosphatase ◽  
Molecular Mass ◽  
High Molecular Mass ◽  
Magnesium Ion ◽  
Kinetic Properties ◽  
Zinc Ions ◽  
Magnesium Ions ◽  
Optimum Conditions ◽  
Ion Concentrations ◽  
Low Magnesium

Abstract We studied the kinetic properties of high- and low-molecular-mass forms of alkaline phosphatase purified from serum and bile, to clarify their interrelationships. They were found to share virtually identical kinetic properties, and to obey the same general kinetics as the liver-derived isoenzyme from serum and the low-molecular-mass isoenzyme from bile with regard to optimum conditions of assay, activation by magnesium ions, inhibition by L-homoarginine, inhibition by nickel and zinc ions, and inactivation by urea. Most of the characteristics such as Km (at low magnesium ion concentrations), Ki for L-homoarginine, and half-life for urea inactivation, were closely similar for low- and high-molecular-mass alkaline phosphatase. We conclude that these forms of alkaline phosphatase in plasma and bile are closely related. We discuss the possible nature of this relationship.

Microbiological Assay of Patulin, Using Bacillus megaterium

1975 ◽  
Vol 58 (3) ◽  
pp. 497-499 ◽  
Author(s):  
William T Stott ◽  
Lloyd B Bullerman
Keyword(s):  
Thin Layer ◽  
Bacillus Megaterium ◽  
Apple Juice ◽  
Test Organism ◽  
Spectrophotometric Assay ◽  
Optimum Conditions ◽  
Liquid Media ◽  
Suitable Test ◽  
Assay Methods ◽  
Quantitative Bioassay

Abstract Bacillus megaterium 1NRRL 1368 was found to be sensitive to patulin and a suitable test organism for an accurate, quantitative bioassay of the toxin. The optimum conditions for the test were determined. The response of the organism to patulin was found to be linear between 2 and 80 μg. When compared to thin layer chromatographic and spectrophotometric assay methods, the bioassay was found to be comparable in accuracy, but less sensitive. The test was found to be sensitive to 1.7 μg patulin. The assay is rapid (12–15 hr), simple, and inexpensive and can be used to verify the toxicity of samples, as well as to quantitatively measure patulin in samples of liquid media, apple juice, and corn.

Alkaline phosphatase of high and low molecular mass in human serum and bile: a comparative study of kinetic properties.

1980 ◽  
Vol 26 (3) ◽  
pp. 451-456 ◽  
Author(s):  
P M Crofton ◽  
A F Smith
Keyword(s):  
Alkaline Phosphatase ◽  
Molecular Mass ◽  
High Molecular Mass ◽  
Magnesium Ion ◽  
Kinetic Properties ◽  
Zinc Ions ◽  
Magnesium Ions ◽  
Optimum Conditions ◽  
Ion Concentrations ◽  
Low Magnesium

Abstract We studied the kinetic properties of high- and low-molecular-mass forms of alkaline phosphatase purified from serum and bile, to clarify their interrelationships. They were found to share virtually identical kinetic properties, and to obey the same general kinetics as the liver-derived isoenzyme from serum and the low-molecular-mass isoenzyme from bile with regard to optimum conditions of assay, activation by magnesium ions, inhibition by L-homoarginine, inhibition by nickel and zinc ions, and inactivation by urea. Most of the characteristics such as Km (at low magnesium ion concentrations), Ki for L-homoarginine, and half-life for urea inactivation, were closely similar for low- and high-molecular-mass alkaline phosphatase. We conclude that these forms of alkaline phosphatase in plasma and bile are closely related. We discuss the possible nature of this relationship.

scholarly journals ISOLATION OF CELLULOLYTIC BACTERIA FROM SOIL AND VALORIZATION OF DIFFERENT LIGNOCELLULOSIC WASTES FOR CELLULASE PRODUCTION BY SUBMERGED FERMENTATION

2021 ◽  
Vol 55 (7-8) ◽  
pp. 821-828
Author(s):  
MISBAH GHAZANFAR ◽  
MUHAMMAD IRFAN ◽  
MUHAMMAD NADEEM ◽  
HAFIZ ABDULLAH SHAKIR ◽  
MUHAMMAD KHAN ◽  
...  
Keyword(s):  
Bacillus Megaterium ◽  
Submerged Fermentation ◽  
Pseudomonas Stutzeri ◽  
Cellulase Production ◽  
Rrna Gene ◽  
Cellulolytic Bacteria ◽  
Bacterial Strains ◽  
Eucalyptus Leaves ◽  
Lignocellulosic Wastes ◽  
Bacillus Flexus

Cellulases are known to convert cellulose into monomeric or dimeric structures, hence playing an important role in bioethanol production, along with their applications in textile and paper industries. This study was directed towards the isolation and screening of cellulase producing bacteria from different soil samples on CMC (carboxymethyl cellulose) agar plates, followed by Gram’s iodine staining. Six strains showed clear zones of hydrolysis on CMC agar plates. Isolates were identified as Bacillus megaterium, Pseudomonas stutzeri, Bacillus aerius, Bacillus paralichniformis, Bacillus flexus, and Bacillus wiedmanni by 16S rRNA gene sequencing. These strains were cultivated by submerged fermentation for cellulase production using various lignocellulosic wastes, such as corn cob, rice husk, wheat straw, seed pods of Bombax ceiba and eucalyptus leaves. Results showed that Pseudomonas stutzeri is the best cellulase producer among these strains. It offered the highest cellulase activity of 170.9±4.1 (IU/mL/min) in media containing eucalyptus leaves after 24 h of incubation at 37 °C, followed by Bacillus paralichniformis, Bacillus wiedmanni, Bacillus flexus, Bacillus aerius and Bacillus megaterium. These bacterial strains and lignocellulosic wastes could be potentially used for industrial exploitation, particularly in biofuels and textiles.

scholarly journals Laccase immobilization via cross-linked aggregate preparation: Characterization, thermodynamic/kinetic properties and application in removal of bisphenol A from solutions

2021 ◽  
Author(s):  
Adedeji Ademakinwa
Keyword(s):  
Bisphenol A ◽  
Kinetic Parameters ◽  
Heat Denaturation ◽  
Heat Inactivation ◽  
Inactivation Kinetics ◽  
Kinetic Properties ◽  
Optimum Conditions ◽  
The Stability ◽  
Laccase Immobilization ◽  
Optimized Conditions

Abstract Fungal laccase from Aureobasidium pullulans was immobilized via cross-linked enzyme aggregate (CLEA) preparation under statistically optimized conditions. The stability of the CLEA to heat inactivation was studied via investigation of its thermodynamic and kinetic parameters. The immobilized enzyme was then deployed in the biodegradation of a bisphenol-A (BPA). The optimum conditions for CLEA preparation resulting in the highest immobilization yield were ammonium sulphate (60% v/v), glutaraldehyde (30 mM), pH (4.5), time (6 h) and temperature (55ºC). The CLEA retained about 51% of its activity after eight catalytic cycles. The optimum pH and temperature of the laccase CLEA were 5.5 and 60ºC respectively. The SEM indicated that the laccase CLEA was type II (unstructured). The data obtained from the heat inactivation kinetics and thermodynamic characterization indicated that the CLEA was stable to heat denaturation than the free enzyme. The kinetic parameters obtained for the CLEA with ABTS as substrate were 101.3 µM, 2.94 µmols-1mg-1 and 0.03 dm3s-1mg-1 for the Km, Kcat and Kcat/Km respectively. The optimum conditions for BPA biodegradation using the CLEA were temperature (55ºC), time (2 h), CLEA (1.0 mg) and BPA concentration (40 mg/L). After the 7th cycle, laccase CLEA retained about 63 ± 2.3% biodegradation efficiency. A heat-resistant laccase CLEA was able to remove BPA from solutions under statistically optimized conditions. The laccase CLEA has properties for other futuristic applications.

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