Purification and Characterization of a Newγ-Glutamylmethylamide-dissimilating Enzyme System fromMethylophagasp. AA-30

1995 ◽  
Vol 59 (4) ◽  
pp. 648-655 ◽  
Author(s):  
Toshio Kimura ◽  
Isao Sugahara ◽  
Katsuyuki Hanai ◽  
Tadashi Asahi
Keyword(s):  
Enzyme System ◽  
Purification And Characterization

Purification and characterization of the E1 component of theClostridium magnum acetoin dehydrogenase enzyme system

1993 ◽  
Vol 64 (1) ◽  
pp. 9-15 ◽  
Author(s):  
Heidrun Lorenzl ◽  
Fred Bernd Oppermann ◽  
Bernhard Schmidt ◽  
Alexander Steinb�chel
Keyword(s):  
Enzyme System ◽  
Purification And Characterization ◽  
Dehydrogenase Enzyme

scholarly journals Thermophilic PHB depolymerase of Stenotrophomonas sp., an isolate from the plastic contaminated site is best purified on Octyl-Sepharose CL-4B

2019 ◽  
Author(s):  
R Z Sayyed ◽  
S J Wani ◽  
S S Shaikh ◽  
Helal F. Al-Harthi ◽  
Asad Syed ◽  
...  
Keyword(s):  
Column Chromatography ◽  
Large Scale ◽  
Enzyme System ◽  
Contaminated Sites ◽  
Contaminated Site ◽  
Purification And Characterization ◽  
Purification Method ◽  
Phb Depolymerase ◽  
Solvent Purification

AbstractThere are numerous reports on PHB depolymerases produced by a wide variety of microorganisms isolated from various habitats, however, reports on PHB depolymerase isolated from plastic contaminated sites are scares. Thermophilic PHB polymerase produced by isolates obtained from plastic contaminated sites is expected to have better relevance for its application in plastic/ bioplastic degradation. Although PHB has attracted commercial significance, the inefficient production and recovery methods, inefficient purification of PHB depolymerase and lack of ample knowledge on PHB degradation by PHB depolymerase have hampered its large scale commercialization. Therefore, to ensure the biodegradability of biopolymers, it becomes imperative to study the purification of the biodegrading enzyme system. We report the production, purification, and characterization of extracellular PHB depolymerase from Stenotrophomonas sp. RZS 7 isolated from a plastic contaminated site. The isolate produced extracellular poly-β-hydroxybutyrate (PHB) depolymerase in the mineral salt medium at 30oC during 4 days of incubation under shake flask condition. Purification of the enzyme was carried out by three different methods using PHB as a substrate. Purification of PHB depolymerase by ammonium salt precipitation, column chromatography, and solvent purification method was successfully carried out. Among the purification method tested, the enzyme was best purified by column chromatography on Octyl-Sepharose CL-4B column with maximum (0.7993 U/mg/ml) purification yield. The molecular weight of purified PHB depolymerase (40 kDa) closely resembled with PHB depolymerase of Aureobacterium saperdae.

CYTOCHROME P450: Nature's Most Versatile Biological Catalyst

2005 ◽  
Vol 45 (1) ◽  
pp. 1-25 ◽  
Author(s):  
Minor J. Coon
Keyword(s):  
Cytochrome P450 ◽  
Enzyme System ◽  
Cytochrome P450 Enzyme ◽  
Purification And Characterization ◽  
P450 Enzyme ◽  
Microsomal Membranes ◽  
Cytochrome P450 Enzyme System ◽  
The Individual ◽  
Reaction Cycles

The author describes studies that led to the resolution and reconstitution of the cytochrome P450 enzyme system in microsomal membranes. The review indicates how purification and characterization of the cytochromes led to rigorous evidence for multiple isoforms of the oxygenases with distinct chemical and physical properties and different but somewhat overlapping substrate specificities. Present knowledge of the individual steps in the P450 and reductase reaction cycles is summarized, including evidence for the generation of multiple functional oxidants that may contribute to the exceptional diversity of the reactions catalyzed.

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