scholarly journals Degradation Potential of Protocatechuate 3,4-Dioxygenase from Crude Extract ofStenotrophomonas maltophiliaStrain KB2 Immobilized in Calcium Alginate Hydrogels and on Glyoxyl Agarose

2014 ◽  
Vol 2014 ◽  
pp. 1-8 ◽  
Author(s):  
Urszula Guzik ◽  
Katarzyna Hupert-Kocurek ◽  
Marta Krysiak ◽  
Danuta Wojcieszyńska
Keyword(s):  
Calcium Alginate ◽  
Enzyme Properties ◽  
Alkaline Ph ◽  
Initial Activity ◽  
Ph Profile ◽  
Alginate Gel ◽  
Chemical Agents ◽  
Optimum Ph ◽  
Immobilization Techniques ◽  
Increased Activity

Microbial intradiol dioxygenases have been shown to have a great potential for bioremediation; however, their structure is sensitive to various environmental and chemical agents. Immobilization techniques allow for the improvement of enzyme properties. This is the first report on use of glyoxyl agarose and calcium alginate as matrixes for the immobilization of protocatechuate 3,4-dioxygenase. Multipoint attachment of the enzyme to the carrier caused maintenance of its initial activity during the 21 days. Immobilization of dioxygenase in calcium alginate or on glyoxyl agarose resulted in decrease in the optimum temperature by 5°C and 10°C, respectively. Entrapment of the enzyme in alginate gel shifted its optimum pH towards high-alkaline pH while immobilization of the enzyme on glyoxyl agarose did not influence pH profile of the enzyme. Protocatechuate 3,4-dioygenase immobilized in calcium alginate showed increased activity towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate. Slightly lower activity of the enzyme was observed after its immobilization on glyoxyl agarose. Entrapment of the enzyme in alginate gel protected it against chelators and aliphatic alcohols while its immobilization on glyoxyl agarose enhanced enzyme resistance to inactivation by metal ions.

scholarly journals Immobilization of alpha-amylase produced by Bacillus circulans GRS 313

2003 ◽  
Vol 46 (2) ◽  
pp. 167-176 ◽  
Author(s):  
Gargi Dey ◽  
Singh Bhupinder ◽  
Rintu Banerjee
Keyword(s):  
Calcium Alginate ◽  
Immobilized Enzyme ◽  
Fold Increase ◽  
Alginate Beads ◽  
Hydrolysis Kinetics ◽  
Initial Activity ◽  
Reaction Conditions ◽  
Bead Size ◽  
Optimum Ph ◽  
Optimum Ph And Temperature

A maltooligosaccharide-forming amylase from B circulans GRS 313 was immobilized by entrapment in calcium alginate beads. The immobilized activity was affected by the size of the bead and bead size of 2mm was found to be most effective for hydrolysis. Kinetics constants, Km and Vmax were estimated and were found to be affected by the bead size. The catalytic activity of the enzyme was studied in presence of various starchy residues and metal ions. HgCl2, CuSO4 and FeCl3 caused inhibition of the enzyme. The reaction conditions, pH and temperature, was optimized using response surface methodology. At the optimum pH and temperature of 4.9 and 57ºC, the apparent activity was 25.6U/g of beads, resulting in almost 2-fold increase in activity. The immobilized enzyme showed a high operational stability by retaining almost 85% of the initial activity after seventh use.

Nitrification and Autotrophic Denitrification in Calcium Alginate Beads

1987 ◽  
Vol 19 (1-2) ◽  
pp. 175-182 ◽  
Author(s):  
Z. Lewandowski ◽  
R. Bakke ◽  
W. G. Characklis
Keyword(s):  
Calcium Carbonate ◽  
Calcium Ions ◽  
Continuous Flow ◽  
Calcium Alginate ◽  
Microbial Respiration ◽  
Flow System ◽  
Alginate Beads ◽  
Alginate Gel ◽  
Gel Beads ◽  
Calcium Alginate Gel

Immobilization of nitrifiers and autotrophic denitrifiers (Thiobacillus denitrificans) within calcium alginate gel was demonstrated. Calcium carbonate reagent was immobilized along with bacteria as the stabilizing agent. Protons released as a result of microbial respiration reacted with calcium carbonate producing calcium ions which internally stabilized the calcium alginate gel. The microbially active gel beads were mechanically stable and active for three months in a continuous flow system without addition of calcium.

Immobilization of glucose oxidase within calcium alginate gel capsules

2001 ◽  
Vol 36 (7) ◽  
pp. 601-606 ◽  
Author(s):  
A Blandino ◽  
M Macı́as ◽  
D Cantero
Keyword(s):  
Glucose Oxidase ◽  
Calcium Alginate ◽  
Alginate Gel ◽  
Calcium Alginate Gel

Calcium alginate gel-entrapped liposomes

2001 ◽  
Vol 17 (1-2) ◽  
pp. 101-105 ◽  
Author(s):  
Masayuki Hara ◽  
Jun Miyake
Keyword(s):  
Calcium Alginate ◽  
Alginate Gel ◽  
Calcium Alginate Gel

scholarly journals Controlled-Release Preparation of Indomethacin Using Calcium Alginate Gel.

1993 ◽  
Vol 16 (11) ◽  
pp. 1164-1168 ◽  
Author(s):  
Sumihiro SHIRAISHI ◽  
Teruko IMAI ◽  
Masaki OTAGIRI
Keyword(s):  
Controlled Release ◽  
Calcium Alginate ◽  
Alginate Gel ◽  
Release Preparation ◽  
Calcium Alginate Gel

scholarly journals Evaluation of optimal conditions for arginase activity in streptozotocin induced diabetic rats

2012 ◽  
Vol 50 (No. 2) ◽  
pp. 69-76 ◽  
Author(s):  
M. Erisir ◽  
E. Ercel ◽  
S. Yilmaz ◽  
S. Ozan
Keyword(s):  
Maximal Activity ◽  
Diabetic Rats ◽  
Arginase Activity ◽  
Female Rats ◽  
Kinetic Properties ◽  
Ph Profile ◽  
Optimum Ph ◽  
Liver And Kidney ◽  
And Control ◽  
Assay Conditions

The assay conditions needed to achieve maximal activity of liver and kidney arginase in diabetic and non-diabetic rats were investigated and compared. The physicochemical and kinetic properties of liver arginase in diabetic and control rats were very similar, those of kidney arginase were significantly different. It was found that preincubation temperature (68&deg;C), preincubation period (20 min), optimum pH (10.1) of liver arginase and K<sub>m</sub> (3.2) for its substrate, L-arginine, did not change in diabetic and non-diabetic rats. As a consequence of diabetes, the optimum Mn<sup>2+</sup> concentration for liver arginase only changed from 1 to 2 mM. Although the preincubation temperature and period for activation of kidney arginase in control rats was unnecessary, they were found to be 56&ordm;C and 12 min in diabetic rats. The pH profile of arginase in kidney of diabetic rats was different from that of control rats. The K<sub>m</sub> value (6.7) of arginase for L-arginine in kidney is unchanged in diabetes whereas a marked decrease in V<sub>max</sub> was found. Optimum Mn<sup>2+</sup> concentration (2 mM) for kidney arginase was unchanged in diabetes. The activity of arginase in liver of diabetic animals was higher 1.5 to 1.7 times than that of controls. Diabetes caused an about 53% decrease of arginase activity in kidney of female rats, 26% in that of males. These findings may suggest an idea that encoded arginases by separate gene loci may be affected differently by the pathological and hormonal status.

scholarly journals Production of Aspartame by Immobilized Thermolysin

2019 ◽  
pp. 1232-1239
Author(s):  
Mohammed A Alsoufi ◽  
Raghad A. Aziz
Keyword(s):  
Reaction Time ◽  
Immobilized Enzyme ◽  
Bentonite Clay ◽  
Optimum Temperature ◽  
Initial Activity ◽  
Reaction Conditions ◽  
Original Activity ◽  
Ph Profile ◽  
Full Activity ◽  
Main Activity

The aim of this study was the production of aspartame by using immobilized thermolysin in bentonite clay. The yield of immobilized thermolysin in bentonite was 92% of the original enzyme amount. pH profile of free and immobilized enzyme was 7.0 and 7.5 respectively which was stable at 6.5-9.0 for 30min. The optimum temperature of both enzymes was 50°C, while they were stable at 65°C for 30min. however, they lost 52.73 and 61.72% from its main activity at 80°C respectively. Immobilized thermolysin has retained all activity within 27 days, but it kept 68.27% of initial activity when stored for 60 days at 4°C whereas, it retained a full activity after 20 continue usage. In addition, it retained 86.53% of its original activity after 30 continuing usages. The yield of produced aspartame was increased with reaction time; it was 9% after 1h and increased gradually to 100% after 10h at reaction conditions.

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