Purification and characterization of NADPH-dependent aldo?keto reductase specific for ?-keto esters from Penicillium citrinum, and production of methyl (S)-4-bromo-3-hydroxybutyrate

2004 ◽  
Vol 66 (1) ◽  
pp. 53-62 ◽  
Author(s):  
N. Itoh ◽  
H. Asako ◽  
K. Banno ◽  
Y. Makino ◽  
M. Shinohara ◽  
...  
Keyword(s):  
Penicillium Citrinum ◽  
Purification And Characterization ◽  
Keto Esters

Production, purification and characterization of nuclease p1 from Penicillium citrinum

2006 ◽  
Vol 41 (6) ◽  
pp. 1276-1281 ◽  
Author(s):  
Ying Guo-Qing ◽  
Lu-E Shi ◽  
Yi Yu ◽  
Tang Zhen-Xing ◽  
Chen Jian-Shu
Keyword(s):  
Penicillium Citrinum ◽  
Purification And Characterization ◽  
Nuclease P1

scholarly journals Production, Purification and Characterization of Extracellular Lipase from a Mutated Strain of Penicillium Citrinum KU613360

2021 ◽  
pp. 111-120
Author(s):  
Lakkakula Bhagya Lakshmi ◽  
M Raghu Ram
Keyword(s):  
Wild Strain ◽  
Strain Improvement ◽  
Lipase Production ◽  
Industrial Applications ◽  
Penicillium Citrinum ◽  
Extracellular Lipase ◽  
Purification And Characterization ◽  
Sds Page ◽  
Guntur District

In the present study lipase production, purification and characterization were carried out with a novel fungal strain of Penicillium citrinum KU613360 isolated from vegetable oil contaminated soil samples collected from oil mills located in and around Guntur District, Andhra Pradesh, India. The strain improvement was carried out by subjecting the strain to both UV and Ethidium Bromide treatments. The wild strain of P. citrinum KU613360 showed maximum lipase activity of 1.053±0.32IUmL-1 on optimized medium and while the mutated strain treated with combination of UV (300 sec) and Et Br (200 µgcm3), recorded the enzyme activity of 4.260±0.011IUmL-1, using the optimised medium at 6.5 pH and 40°C temperature. Thus, a 404% enhancement in the activity was achieved by using induced mutation on wild strain of P. citrinum KU613360. The molecular weight of the purified lipase from the mutated strain was found to be 35 kDa, when analysed on SDS PAGE. From our results it was concluded that the mutated strain has considerable capability and potentiality to be used in various industrial applications.

Purification and characterization of pectin lyase secreted by Penicillium citrinum

2009 ◽  
Vol 74 (7) ◽  
pp. 800-806 ◽  
Author(s):  
S. Yadav ◽  
P. K. Yadav ◽  
D. Yadav ◽  
K. D. S. Yadav
Keyword(s):  
Penicillium Citrinum ◽  
Pectin Lyase ◽  
Purification And Characterization

Purification and characterization of phosphoglucomutase from peas

1994 ◽  
Vol 92 (3) ◽  
pp. 479-486 ◽  
Author(s):  
Cynthia M. Galloway ◽  
W. Mack Dugger
Keyword(s):  
Purification And Characterization

Purification and Characterization of Tissue-Type Plasminogen Activator in Maxillary Mucosa with Chronic Inflammation

1985 ◽  
Vol 54 (02) ◽  
pp. 485-489 ◽  
Author(s):  
Yukiyoshi Hamaguchi ◽  
Masuichi Ohi ◽  
Yasuo Sakakura ◽  
Yasuro Miyoshi
Keyword(s):  
Plasminogen Activator ◽  
Chronic Inflammation ◽  
Gel Filtration ◽  
Potassium Acetate ◽  
Tissue Type ◽  
Purification And Characterization ◽  
Tissue Type Plasminogen Activator ◽  
Urokinase Inhibitor ◽  
Type Plasminogen Activator

SummaryTissue-type plasminogen activator (TPA) was purified from maxillary mucosa with chronic inflammation and compared with urokinase. Purification procedure consisted of the extraction from delipidated mucosa with 0.3M potassium acetate buffer (pH 4.2), 66% saturation of ammonium sulfate, zinc chelate-Sepharose, concanavalin A-Sepharose and Sephadex G-100 gel filtration chromatographies.The molecular weight of the TPA was approximately 58,000 ± 3,000. Its activity was enhanced in the presence of fibrin and was quenched by placental urokinase inhibitor, but not quenched by anti-urokinase antibody. The TPA made no precipitin line against anti-urokinase antibody, while urokinase did.All these findings indicate that the TPA in maxillary mucosa with chronic inflammation is immunologically dissimilar to urokinase and in its affinity for fibrin.

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

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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