A novel and enantioselective epoxide hydrolase from Aspergillus brasiliensis CCT 1435: Purification and characterization
نویسندگان
چکیده
منابع مشابه
Cloning and molecular characterization of a soluble epoxide hydrolase from Aspergillus niger that is related to mammalian microsomal epoxide hydrolase.
Aspergillus niger strain LCP521 harbours a highly processive epoxide hydrolase (EH) that is of particular interest for the enantioselective bio-organic synthesis of fine chemicals. In the present work, we report the isolation of the gene and cDNA for this EH by use of inverse PCR. The gene is composed of nine exons, the first of which is apparently non-coding. The deduced protein of the A. nige...
متن کاملPurification and identification of an epoxide hydrolase from equine liver.
In the horse, drug metabolism has been shown to be complex, but little is known about the proteins involved in these processes [l]. As a result of work on the purification of equine Cytochrome P450 enzymes, an epoxide hydrolase has been purified [2]. Epoxide hydrolases catalyse the hydration of biologically active epoxides formed during the metabolism of many drugs and mutagenic compounds [3]. ...
متن کاملA xyloglucan-specific family 12 glycosyl hydrolase from Aspergillus niger: recombinant expression, purification and characterization.
A new GH12 (glycosyl hydrolase 12) family XEG [xyloglucan-specific endo-beta-1,4-glucanase (EC 3.2.1.151)] from Aspergillus niger, AnXEG12A, was overexpressed, purified and characterized. Whereas seven xyloglucanases from GH74 and two xyloglucanases from GH5 have been characterized previously, this is only the third characterized example of a GH12 family xyloglucanase. GH12 enzymes are structur...
متن کاملPARTIAL PURIFICATION AND CHARACTERIZATION OF B-GALACTOSIDASE FROM ASPERGILLUS NIGER UV-5
The enzyme pgalactosidase from a mutant strain of A. niger UV-5 was partially purified using ammonium sulfate and acetone. The saturation range of 60-80% ammonium sulfate was found to yield 60.5% enzyme recovery with 2.4 fold purification. Acetone precipitation at enzyme: acetone ratio of 1 : 1.5 brought about a higher yield i.e. 68% and three-fold purification. The combined procedures of ...
متن کاملMicrosomal epoxide hydrolase of rat liver. Purification and characterization of enzyme fractions with different chromatographic characteristics.
Microsomal epoxide hydrolase was purified from rat liver, and different fractions of the purified enzyme, which varied in their contents of phospholipid, were obtained by ion-exchange chromatography. One fraction (A), which did not bind to CM-cellulose, had a high phospholipid content, and a second fraction (B), which was eluted from CM-cellulose at high ionic strength, had a low phospholipid c...
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ژورنال
عنوان ژورنال: Protein Expression and Purification
سال: 2013
ISSN: 1046-5928
DOI: 10.1016/j.pep.2013.08.001