Recombinant Mycobacterium sp. strain MR65 harboring dszABCD genes was used to desulfurize alkyl dibenzothiophenes (Cx-DBTs) in n-hexadecane. The specific desulfurization activity for 2,4,6,8-tetraethyl DBT (C8-DBT) by DszC enzyme was about twice that for 4,6-dipropyl DBT (C6-DBT). However, the degradation rate of 2,4,6,8-tetraethyl DBT in n-hexadecane by resting cells of strain MR65 was only about 40% of that of 4,6-dipropyl DBT. These results indicated that the desulfurization ability for Cx-DBTs by resting cells depends on carbon number substituted at positions 4 and 6 and that the rate-limiting step in the desulfurization reaction of highly alkylated Cx-DBTs is the transfer process from the oil phase into the cell.
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http://dx.doi.org/10.1023/a:1025020003953 | DOI Listing |
J Biosci Bioeng
November 2005
Bio-Refining Process Laboratory, Technical Cooperation Department, Japan Cooperation Center Petroleum, 1900 Sodeshi-cho, Shimizu-shi, Shizuoka 424-0037, Japan.
Rhodococcus erythropolis strain KA2-5-1 is unable to desulfurize 4,6-dipropyl dibenzothiophene (DBT) in the oil phase. The dsz desulfurization gene cluster from R. erythropolis strain KA2-5-1 was transferred into 22 rhodococcal and mycobacterial strains using a transposon-transposase complex.
View Article and Find Full Text PDFBiotechnol Lett
September 2003
Bio-Refining Process Laboratory, Technical Cooperation Department, Japan Cooperation Center, Petroleum, 58F Sun-shine 60, 3-1-1 Ikebukuro, Toshima-ku, Tokyo 170-6058, Japan.
Recombinant Mycobacterium sp. strain MR65 harboring dszABCD genes was used to desulfurize alkyl dibenzothiophenes (Cx-DBTs) in n-hexadecane. The specific desulfurization activity for 2,4,6,8-tetraethyl DBT (C8-DBT) by DszC enzyme was about twice that for 4,6-dipropyl DBT (C6-DBT).
View Article and Find Full Text PDFBiotechnol Lett
May 2003
Bio-Refining Process Laboratory, Technical Cooperation Department, Japan Cooperation Center, Petroleum, 1900 Sodeshi-cho, Shimizu-shi, Shizuoka 424-0037, Japan.
Recombinant Mycobacterium sp. strain MR65 carrying dszABCD genes was used for desulfurization of 10-methylbenzo[b]naphtho[2,1-d]thiophene (10-methyl BNT) in the hexadecane phase. The specific activity was 25% of that of dibenzothiophene (DBT).
View Article and Find Full Text PDFBiochem J
April 1991
Department of Biochemistry, Gifu Pharmaceutical University, Japan.
The immunological relationship of two forms of dihydrodiol dehydrogenase (DD) in pig lens to pig muscle aldose reductase and kidney aldehyde reductase has been studied. Although the minor enzyme form, a monomer of Mr 35,000, was identical with aldose reductase, the major enzyme form, a dimer of Mr 65,000, was distinct from the two reductases. The two enzyme species, although their amounts were low, were distributed in the cornea, iris-ciliary body, retina and choroid of the pig eye.
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