scholarly journals The Role of Ion Exchange Chromatography in Purification and Characterization of Molecules

10.5772/52537 ◽  
2012 ◽  
Author(s):  
Hidayat Ullah
Keyword(s):  
Ion Exchange ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Purification And Characterization

Purification and Characterization of Laccase from Curvularia trifol

2010 ◽  
Vol 113-116 ◽  
pp. 2215-2219
Author(s):  
Jie Zhang ◽  
Jing Ren ◽  
Yang Yu ◽  
Bin Song Wang
Keyword(s):  
Enzyme Activity ◽  
Ion Exchange ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Recycling Rate ◽  
Relative Molecular Mass ◽  
Optimal Temperature ◽  
Purification And Characterization ◽  
Alizarin Red

Electrophoretic pure lacquer enzymes were obtained from the thick enzyme of Gladiolus Curvularia trifol with grading precipitation and DEAE2-Cellulose ion exchange chromatography. The overall recycling rate of enzyme activity was 14.97% and the purification reached 2.96 times. The relative molecular mass of enzyme was 92.3Kda. The optimal temperature and pH were 40°C and 3.5, respectively. The Km of ABTS catalyzed by laccase was 1.11× 10- 5mol L-1. Alizarin red and Congo red could be degradated by purified laccase effectively without the participation of small molecule amboceptor. Alizarin red could be degradated by 80% with its being affected by 1000U/L of enzyme activity for 70h, which revealed the huge potentiality of Gladiolus Curvularia trifol and laccase in the degradation of dye.

scholarly journals Purification and Characterization of Cellulase from Termite Ametermes eveuncifer (Silverstri) Soldiers

2016 ◽  
Vol 9 (1) ◽  
pp. 1 ◽  
Author(s):  
B. S. Fagbohunka ◽  
R. E. Okonji ◽  
Ayinla Zainab Adenike
Keyword(s):  
Ion Exchange ◽  
Specific Activity ◽  
Ion Exchange Chromatography ◽  
Maximum Activity ◽  
Exchange Chromatography ◽  
Purification And Characterization ◽  
Ammonium Sulphate Precipitation ◽  
Percentage Yield ◽  
Termite Soldiers

Cellulase enzyme was purified and characterized from termite soldiers (Ametermes eveuncifer) using 70% ammonium sulphate precipitation, ion exchange chromatography and affinity chromatography. The enzyme isolated had a specific activity of 5.04 U/mg with a percentage yield of 11.7%. The enzyme showed maximum activity at 500C and pH 8. The enzyme was not inhibited by Ba2+ at a concentration of 1mM and Pb2+ at 10 mM concentration but was inhibited by other metal ions at 1 mM and 10 mM concentrations of their salts (NaCl, KCl, MnCl2, and NiCl2),

scholarly journals PURIFICATION AND CHARACTERIZATION OF β-GALACTOSIDASE OF `FUJI' APPLES

HortScience ◽  
1992 ◽  
Vol 27 (6) ◽  
pp. 653f-653
Author(s):  
Seung-Ryeul Shin ◽  
Jae-Kyun Byun ◽  
Kyung-Ho Chang
Keyword(s):  
Ion Exchange ◽  
Malus Domestica ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Purification And Characterization ◽  
Biochemical Methods ◽  
Stable Temperature ◽  
Optimum Ph

β-Galactosidase was purified from apple, Malus domestica Borkh, cv. Fuji by gel filtration, CM cellulose ion exchange chromatography, and characterizied by means of several biochemical methods. One form of β-Galactosidase was detected and the Km and Vmax values were calculated to be 0.035 and 0.036 mM with para-nitrophenyl-β-D-galactoside lmM/15min., respectively. The β-galactosidase was active between pH 3 and 7 with the optimum pH of about 4-5. The stable temperature for β-galactosidase was lower than 45°C with 30°C optimum. The β-galactosidase activities were inhibited by Ag*. EDTA and SDS.

Proteolysis in Heterocyst-Forming Cyanobacteria: Characterization of a Further Enzyme with Trypsin-Like Specificity, and of a Prolyl Endopeptidase from Anabaena variabilis

1994 ◽  
Vol 49 (1-2) ◽  
pp. 70-78 ◽  
Author(s):  
Ulrike Strohmeier ◽  
Christian Gerdes ◽  
Wolfgang Lockau
Keyword(s):  
Ion Exchange ◽  
Proteolytic Enzymes ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Anabaena Variabilis ◽  
Prolyl Endopeptidase ◽  
Cyanobacterium Anabaena

Soluble extracts of the cyanobacterium Anabaena variabilis ATCC 29413 and an engineered mutant that lacks an intracellular protease cleaving after Lys and Arg (Maldener, Lockau, Cai, and Wolk, Mol. Gen. Genet. 225, 113-120 (1991)) were separated by ion exchange chromatography, and protease profiles determined using azocasein, Nα-benzoyl-ᴅ,ʟ arginine- 4-nitroanilide and N-carbobenzoxy-glycyl-ʟ-proline-4-nitroanilide as substrates. A second enzyme cleaving at the carboxyl side of lysine and arginine, and a prolyl endopeptidase were detected, enriched and characterized. Both proteolytic enzymes appear to be located in the periplasm.

scholarly journals Biochemical Characterization of a Thiol-Activated, Oxidation Stable Keratinase from Bacillus pumilus KS12

2010 ◽  
Vol 2010 ◽  
pp. 1-7 ◽  
Author(s):  
Rinky Rajput ◽  
Richa Sharma ◽  
Rani Gupta
Keyword(s):  
Ion Exchange ◽  
Bacillus Pumilus ◽  
Biochemical Characterization ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Amidolytic Activity ◽  
Alkaline Serine Protease ◽  
Sds Page ◽  
Temperature Optima

An extracellular keratinase from Bacillus pumilus KS12 was purified by DEAE ion exchange chromatography. It was a 45 kDa monomer as determined by SDS PAGE analysis. It was found to be an alkaline, serine protease with pH and temperature optima of 10 and 60C, respectively. It was thiol activated with two- and eight-fold enhancement in presence of 10 mM DTT and β-mercaptoethanol, respectively. In addition, its activity was stimulated in the presence of various surfactants, detergents, and oxidizing agents where a nearly 2- to 3-fold enhancement was observed in presence of H2O2 and NaHClO3. It hydrolyzed broad range of complex substrates including feather keratin, haemoglobin, fibrin, casein,and α-keratin. Analysis of amidolytic activity revealed that it efficiently cleaved phenylalanine → leucine → alanine- p-nitroanilides. It also cleaved insulin B chain between Val2- Asn3, Leu6-Cys7 and His10-Leu11 residues.

scholarly journals Studies on the protein-bound chondroitin sulphate of bovine cortical bone

1968 ◽  
Vol 107 (1) ◽  
pp. 41-49 ◽  
Author(s):  
G. M. Herring
Keyword(s):  
Ion Exchange ◽  
Cortical Bone ◽  
Chondroitin Sulphate ◽  
Bone Sialoprotein ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Mild Conditions ◽  
The Third ◽  
Apparent Homogeneity

A fraction containing chondroitin sulphate, isolated from bovine cortical bone under mild conditions, was separated by ion-exchange chromatography into three fractions with apparent homogeneity on electrophoresis and ultracentrifugation. Two of these appeared to consist of chondroitin sulphate bound to a glycoprotein ‘core’ that had similarities to the bone sialoprotein described previously. The differences in composition of the two fractions were considered to be due to variation in the number or lengths of the polysaccharide chains. The presence of xylose and the alkali-lability of the bond between protein and polysaccharide suggested the presence of a xylosylserine linkage. The third fraction had the properties of a relatively pure chondroitin sulphate which contained a small amount of peptide. These fractions differed considerably from the protein–polysaccharide complexes of epiphysial and other cartilages, and their relevance to the possible role of glycosaminoglycans is discussed.

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