Purification and Characterization of a Bioscouring Pectate Lyase from Paenibacillus sp. WZ008 with High Activity on Pectin

An extracellular pectate lyase was purified from the culture supernatant of Paenibacillus sp. WZ008 grown in the pectin-containing medium. The enzyme was purified to homogeneity in three steps and found to have a molecular weight of around 45 kDa. Highly methylated pectin was the optimum substrate in the case of no Ca2+ addition while the enzyme exhibited the maximal activity on polygalacturonic acid in the presence of 4 mM Ca2+. The purified enzyme demonstrated the optimum activity at a temperature range of 55-60°C and pH 9.6. The Ca2+ ion enhanced the enzyme activity but Mn2+, Ba2+ and EDTA strongly inhibited it.

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Partial purification and characterization of xylanase from Bacillus cereus X3

Baghdad Science Journal ◽

10.21123/bsj.11.2.1056-1061 ◽

2014 ◽

Vol 11 (2) ◽

pp. 1056-1061

Author(s):

Baghdad Science Journal

Keyword(s):

Bacillus Cereus ◽

Maximal Activity ◽

Partial Purification ◽

Purification And Characterization ◽

Xylanase Production ◽

Optimum Activity ◽

Biology Department ◽

Characterization Study ◽

Quantitative Screening

Three strain of Bacillus cereus were obtained from soil sours Laboratories of Biology Department/ College of Science/ University of Baghdad. The bacteria secreted extracellular xylanase in liquid cultur the test ability of xylanase production from these isolates was studied semi quantitative and quantitative screening appeared that Bacillus cereus X3 was the highest xylanase producer. The enzyme was partial purification 191 fold from cultur by reached step by 4 U/mg proteins by ammonium sulfat precipitation 80%, Ion exchang DEAE-cellulos chromatography Characterization study of the partial purifation enzyme revealed that the enzyme had a optimum activity pH8 and activity was stable in the pH rang (8-10) for 30min. maximal activity was attained at 50C

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Comparison of mitochondrial and cytosolic tRNA nucleotidyltransferases from Triticum aestivum

Canadian Journal of Botany ◽

10.1139/b98-206 ◽

1999 ◽

Vol 77 (2) ◽

pp. 230-239

Author(s):

Raffaela Vicaretti ◽

Paul BM Joyce

Keyword(s):

Triticum Aestivum ◽

High Activity ◽

Maximal Activity ◽

Partial Purification ◽

Elution Profile ◽

Mitochondrial Enzyme ◽

Alkaline Ph ◽

Purification And Characterization ◽

Purification Scheme

Here we report the partial purification and characterization of wheat mitochondrial ATP (CTP):tRNA nucleotidyltransferase (EC 2.7.7.25). Our purification scheme involves ammonium sulfate fractionation and chromatography on anion-exchange, hydroxyapatite, and affinity columns. Our results indicate that the enzyme is stable over a broad range of temperatures with highest activity at 37°C. High activity is seen at alkaline pH with a maximum at pH 9. The enzyme exhibits maximal activity in the presence of 10 mM MgCl2 and is inhibited by (at least) 100 mM NaCl. We also show that a second form of this enzyme exists in the wheat cytosolic fraction. This enzyme shares many features with the mitochondrial enzyme but differs from the mitochondrial enzyme in its elution profile from hydroxyapatite and in its response to manganese.Key words: tRNA nucleotidyltransferase, wheat, mitochondria.

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Molecular characterization of an endo-type chitosanase from the fish pathogenRenibacteriumsp. QD1

Journal of the Marine Biological Association of the United Kingdom ◽

10.1017/s0025315413001859 ◽

2014 ◽

Vol 94 (4) ◽

pp. 681-686 ◽

Cited By ~ 3

Author(s):

Peichuan Xing ◽

Dan Liu ◽

Wen-Gong Yu ◽

Xinzhi Lu

Keyword(s):

Molecular Weight ◽

Enzyme Activity ◽

Specific Activity ◽

Fermentation Broth ◽

Maximal Activity ◽

Optimum Temperature ◽

Sds Page ◽

Ph Range ◽

Tlc Analysis

Renibacteriumsp. QD1, a bacteria strain capable of hydrolysing chitosan, was isolated from the homogenate of small crabs. An extracellular chitosanase, Csn-A, was purified from the QD1 fermentation broth. The enzyme was purified to homogeneity, with a yield of eight-fold, 67% recovery and a specific activity of 1575 U/mg proteins. The molecular weight of Csn-A was estimated to be 26.1 kDa by SDS-PAGE. Unlike other chitosanases, the purified Csn-A displayed maximal activity at a pH range of 5.3–6.5, and it was stable in a broad pH range of 5.0–10.0. The optimum temperature for chitosanlytic activity was 55°C. The enzyme activity was strongly stimulated by Mn2+but inhibited by Fe3+, Cu2+, Al3+, Zn2+and SDS. TLC analysis demonstrated that Csn-A hydrolysed N-deacetylated polymeric glucosamines into chito-biose and -triose in an endo-type manner. The amino acid seuquence of Csn-A showed close identity with an uncharacterized chitosanase of strain ATCC33209.

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Purification and characterization of an aspartyl proteinase from dry jack pine seeds

Seed Science Research ◽

10.1017/s0960258500000817 ◽

1991 ◽

Vol 1 (3) ◽

pp. 139-147 ◽

Cited By ~ 16

Author(s):

Jacqueline Bourgeois ◽

L. Malek

Keyword(s):

Molecular Weight ◽

High Activity ◽

High Molecular Weight ◽

Pinus Banksiana ◽

Jack Pine ◽

Purification And Characterization ◽

Hydrolysis Products ◽

Early Germination ◽

Pepstatin A

AbstractA high-molecular-weight aspartyl proteinase complex, sensitive to pepstatin A was purified to near electrophoretic homogeneity from dry seeds ofjack pine (Pinus banksiana, Lamb.). Two partial activities, endo-and exo-proteinolytic, were associated with the complex, judged by the analysis of haemoglobin hydrolysis products. The high activity of this enzyme in dry jack pine seed suggests a possible function in early germination.

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Prothrombin Metz : Purification and Characterization of a Variant of Human Prothrombin

10.1055/s-0038-1665670 ◽

1979 ◽

Author(s):

M Ribieto ◽

J Elion ◽

D Labie ◽

F Josso

Keyword(s):

Molecular Weight ◽

Gel Electrophoresis ◽

Polyacrylamide Gel Electrophoresis ◽

Factor Xa ◽

Polyacrylamide Gel ◽

Cleavage Pattern ◽

Purification And Characterization ◽

Double Immunodiffusion ◽

The Family

For the purification of the abnormal prothrombin (Pt Metz), advantage has been taken of the existence in the family of three siblings who, being double heterozygotes for Pt Metz and a hypoprothrombinemia, have no normal Pt. Purification procedures included barium citrate adsorption and chromatography on DEAE Sephadex as for normal Pt. As opposed to some other variants (Pt Barcelona and Madrid), Pt Metz elutes as a single symetrical peak. By SDS polyacrylamide gel electrophoresis, this material is homogeneous and appears to have the same molecular weight as normal Pt. Comigration of normal and abnormal Pt in the absence of SDS, shows a double band suggesting an abnormal charge for the variant. Pt Metz exhibits an identity reaction with the control by double immunodiffusion. Upon activation by factor Xa, Pt Metz can generate amydolytic activity on Bz-Phe-Val-Arg-pNa (S2160), but only a very low clotting activity. Clear abnormalities are observed in the cleavage pattern of Pt Metz when monitored by SDS gel electrophoresis. The main feature are the accumulation of prethrombin l (Pl) and the appearance of abnormal intermediates migrating faster than Pl.

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