Biodesulfurization

Current Opinion in Microbiology

Volumn 2, Issue 3, 1999, Pages 257-264

  McFarland, Beverly L ^a  

^a MicroBioTech Consulting   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIBENZOTHIOPHENE DERIVATIVE; FOSSIL FUEL;

BIODIVERSITY; DESULFURIZATION; ENZYME SPECIFICITY; GENETIC ENGINEERING; GENETIC REGULATION; MICROORGANISM; MOLECULAR GENETICS; PETROCHEMICAL INDUSTRY; REVIEW;

EID: 0033151649     PISSN: 13695274     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1369-5274(99)80045-9     Document Type: Article

References (62)

1. Atlas RM, Boron DJ, Deever WR, Johnson AR, McFarland BL, Meyer JA: Biodesulfurization of Gasoline - A Technology Roadmap. Coordinating Research Council; Atlanta Georgia: 1998.[CRC Report no. 615, CRC Project no. E-7c, pp1-82.] A multidisciplinary view of biodesulfurization options for gasoline, including sulfur speciation throughout refinery streams, biochemistry and genetics of desulfurization, bioreactor design concepts and process economic estimations. This document also presents technology roadmaps of possible routes to achieve gasoline biodesulfurization processes within the next 5-6 years and determines that any bioprocess must be below the 1.5 cent/gallon of total pool gasoline cost estimated for emerging chemical/physical desulfurization processes.
2. Shong RG: Bioprocessing of crude oil. In 217th ACS National Meeting Proceedings: 1999 March 21-25: Anaheim, CA. American Chemical Society 1999, 44:1-9.
3. Monticello DJ: Riding the fossil fuel biodesulfurization wave. CHEMTECH 1998, 28:38-45. This article presents information on research funding for biodesulfurization and provides the Web site address for the University of Minnesota biocatalysis/biodegradation database with details of the different desulfurization pathways (http://www.labmed.umn.edu/umbbd/index.html).
4. McFarland BL, Boron DJ, Deever WR, Meyer JA, Johnson AR, Atlas RM: Biocatalytic sulfur removal from fuels: Applicability for producing low sulfur gasoline. Critical Rev Microbiol 1998, 24:99-147.
5. Speight JG: The Desulfurization of Heavy Oils and Residua. New York: Marcel Dekker; 1981.
6. CONCAWE: Motor Vehicle Emission Regulations and Fuel Specifications. Brussels: Oil Companies European Organization for Environmental and Health Protection (CONCAWE); 1994. [Report no. 4/94, 1994 update.]
7. Ohshiro T, Izumi Y: Microbial desulfurization of organic sulfur compounds in petroleum. Biosci Biotechnol Biochem 1999, 63:1-9. This review summarizes biodesulfurization progress from the basic and practical point of view.
8. Grossman MJ: Microbial removal of organic sulfur from fuels: A review of past and present approaches. In Hydrotreating Technology for Pollution Control. Catalysts, Catalysis, and Processes. Edited by Ocelli ML, Chianelli R. New York: Marcel Decker, Inc.; 1996:345-359.
9. Premuzic ET, Lin MS, Bohenek M, Zhou WM: Bioconversion reactions in asphaltenes and heavy crude oils. Energy and Fuels 1999, 13:297-304. This paper presents mass balance information and uses a factorial approach to experimentation with four heavy crude oils under going treatment with different biocatalysts at 40-65°C. They observed increases in saturates, and decreases in aromatics and resins along with the 20-40% reductions in sulfur, nitrogen, oxygen and metals (nickel, vanadium). The research also highlights some biological variability issues although it is hard to put this into microbiological perspective because the biocatalysts are not identified by genus or species.
10. Grossman MJ, Lee MK, Prince RC, Garrett KK, George GN, Pickering IJ: Microbial desulfurization of a crude oil middle-distillate fraction: Analysis of the extent of sulfur removal and the effect of removal on remaining sulfur. Appl Environ Microbiol 1999, 65:181-188. State-of-the-art sulfur analytical methods document that up to 30% of the total sulfur in middle distillate was removed by biotreatment with Rhodococcus ECRD-1. Compounds across the entire boiling range were affected. Over 50% of the remaining sulfur was in an oxidized form suggesting the substrate range of the sulfur oxidation enzymes is broader than that of the enzymes involved in carbon-sulfur bond cleavage. Thiophenic and sulfidic sulfur compounds were removed in approximately equal amounts. A problem with unexpected alkane utilization was eliminated by decane addition, which allowed an accurate measure of sulfur removal as the oil removal was eliminated. The authors suggest the substrate range of the desulfurization enzymes and/or bioavailability, not the sulfur requirements of the cell, limit further desulfurization and suggest that broadening the substrate range of the carbon-sulfur cleavage enzymes to include those oxidized compounds present in the treated oils should allow for considerably more desulfurization of middle-distillate oils.
11. Pacheco MA, Lange EA, Pienkos PT, Yu LQ, Rouse MP, Lin Q, Linguist LK: Recent advances in biodesulfurization of diesel fuel. NPRA AM-99-27, 1999 National Petrochemical and Refiners Association, Annual Meeting, March 21-23; San Antonio, Texas. 1999:1-26. Interesting update of the status of Energy Biosystems Corporation proprietary biodesulfurization (BDS) technology, including the latest modifications to the process design, updated economics, and the proposals for converting BDS chemistry into saleable products. Also of interest is the documentation of the stages of biocatalyst and bioprocess improvements over time.
12. Lizama HM, Wilkins LA, Scott TC: Dibenzothiophene sulfur can serve as sole electron acceptor during growth by sulfate-reducing bacteria. Biotechnol Lett 1995, 17:113-116.
13. Kim BH, Kim HY, Kim TS, Park DH: Selectivity of desulfurization activity of Desulfovibrio desulfuricans M6 on different petroleum products. Fuel Processing Technol 1995, 43:87-94.
14. Armstrong SM, Sankey BM Voordouw G: Conversion of dibenzothiophene to biphenyl by sulfate-reducing bacteria isolated from oil field production facilities. Biotechnol Lett 1995, 17:1133-1137.
15. 2S production.
16. Gilbert SC, Morton J, Buchanan S, Oldfield C, McRoberts A: Isolation of a unique benzothiophene-desulphurizing bacterium, Gordona sp. strain 213E (NCIMB 40816), and characterization of the desulphurization pathway. Microbiology 1998, 144:2545-2553. This paper documents that Gordona sp. isolated on benzothiophene enrichment medium had desulfurization activities specific to their enrichment substrates. Gordona sp. strain 213E (NCIMB 40816), isolated on benzothiophenes as the sole sulfur source, desulfurizes benzothiophenes by activation of sulfur to facilitate thiophene ring opening and desulfination. It does not desulfurize dibenzothiophenes (DBTs), and R. erythropolis IGTS8 did not desulfurize benzothiophene. The DBT and benzothiophene desulfurization mechanisms differ crucially in the nature of the sulfinic acid generated following thiophene ring-opening, and the reactions are complementary. No mineralization of DBT carbon was observed.
17. Izumi Y, Ohshiro T, Ogino H, Hine Y, Shimao M: Selective desulfurization of dibenzothiophene by Rhodococcus erythropolis D-1. Appl Environ Microbiol 1994, 60:223-226.
18. Lee MK, Senius JD, Grossman MJ. Sulfur-specific microbial desulfurization of sterically hindered analogs of dibenzothiphene. Appl Environ Microbiol 1995, 61:4362-4366.
19. Denis-Larose C, Labbe D, Bergeron H, Jones AM, Greer CW, al Hawari J, Grossman MJ, Sankey BM, Lau PC: Conservation of plasmid-encoded dibenzothiphene desulfurization genes in several rhodococci. Appl Environ Microbiol 1997, 63:2915-2919. The cloned sulfur oxidation genes (sox also known as dsz) for dibenzothiophene (DBT) desulfurization from R. erythropolis IGTS8 were used in Southern hybridization and PCR experiments to establish the close relatedness of different desulfurizing microorganisms. They also identified that by the criteria of plasmid content, size and distribution of insertion sequence elements that Rhodococcus strain X309 and related isolates are genetically distinct from the prototype IGTS8 desulfurization strain. This study provides additional evidence that insertion elements as well as pulsed field gel electrophoresis (PFGE) techniques are useful molecular tools for strain differentiation.
20. Omori T, Monna LS, Kodama T: Desulfurization of alkyl and aromatic sulfides and sulfonates by dibenzothiophene desulfurizing Rhodococcus sp. Stain SY-1. Appl Environ Microbiol 1995, 59:1195-1198.
21. Purdy RF, Lepo JE, Ward B: Biodesulfurization of organic-sulfur compounds. Curr Microbiol 1993, 27:219-222.
22. Constanti M, Giralt J, Bordons A: Degradation and desulfurization of dibenzothiophene sulfone and other sulfur compounds by Agrobacterium MC501 and a mixed culture. Enzyme Microb Technol 1996, 19:214-219.
23. Nekodzuka S, Toshiaki N, Nakajima-Kambe T, Nobura N, Lu J, and Nakahara Y: Specific desulfurization of dibenzothiophene by Mycobacterium strain G3. Biocatalysis Biotransformation 1997, 15:21-27.
24. Rhee SK, Chang JH, Chang YK, Chang HN: Desufurization of dibenzothiophene and diesel oils by a newly isolated Gordona strain, CYKS1. Appl Environ Microbiol 1998, 64:2327-2331.
25. Dudley MW, Frost JW: Biocatalytic desulurization of arylsulfonates. Bioorg Med Chem 1994, 2:681-690.
26. Constanti M, Giralt J, Bordons A: Desulfurization of dibenzothiphene by bacteria. World J Microbiol Biotechnol 1994, 10:510-516.
27. Wang P, Krawiec S: Desulfurization of dibenzothiophene to 2-hydroxybiphenyl. Arch Microbiol 1994, 161:266-271.
28. Konishi J, Ishii Y, Onaka T, Okumura K, Suzuki M: Thermophilic carbon-sulphur bond targeted biodesulfurization. Appl Environ Microbiol 1997, 63:3164-3169. The first report of thermophilic biodesulfurization of dibenzothiophenes and methylated derivatives at temperatures up to 60°C by two Paenibacillus spp.
29. Ishii Y, Kobayashi J, Onada T, Okumura K, Suzuki M: Desulfurization of petroleum by the use of biotechnology. Nippon Kagaku Kaishi, 1998, Jun:373-381. [In Japanese.]
30. Schlenk D, Bevers RJ, Vertino AM, Cerniglia CE: P450 catalyzed S-oxidation of dibenzothiphene by Cunninghamella elegans. Xenobiotica 1994, 24:1077-1083.
31. 35S] dibenzothiophene.
32. van Berkel WJH, Muller F: Flavin-dependent monooxygenases with special reference to p-hydroxybenzoate hydroxylase. In Chemistry and Biochemistry of Flavoenzymes, vol II. Edited by Muller F. Boca Raton: CRC Press; 1991:1-29.
33. Murrell JC: Molecular genetics of methane oxidation. Biodegradation 1994, 5:145-159.
34. 2 from FMN:NADPH oxidreductase for oxygenation. They also reported that a recombinant Pseudomonas putida strain KT244o with a plasmid encoding dszA, dszC, and a flavin reductase gene is much more active than a strain with only dszA and dszC suggesting that a reductase must be present in R. erythropolis IGTS8 or alternate hosts for full expression of the desulfurization phenotype.
35. Gray KA, Pogrebinsky OS, Mrachko GT, Lei X, Monticello DJ, Squires CH: Molecular mechanisms of biocatalytic desulfurization of fossil fuels. Nat Biotechnol 1996 14:1705-1709.
36. Nagy I, Verheijen S, Schoofs G, Vanderleyden J, DeMot R: Thiocarbamate-inducible alcohol:N-N'-dimethyl-4-nitrosoaniline oxidoreductase of Rhodococcus sp. NI86-21. Biotekhnologiya 1995, 7-8:155-158.
37. Ohshiro T, Kanbayashi Y, Hine Y, Izumi Y: Involvement of flavin coenzyme in dibenzothiophene degrading enzyme system from Rhodococcus erythropolis D-1. Biosci Biotechnol Biochem 1995, 59:1349-1351.
38. van der Ploeg JR, Cummings NJ, Leisinger T, Connerton IF: Bacillus subtilis genes for the utilization of sulfur from aliphatic sulfonates. Microbiology 1998, 144:2555-2561.
39. Cook AM, Laue, H, Junker F: Microbial desulfonation. FEMS Microbiol Reviews 1999, 22:399-419.
40. Beil S, Kehrli H, James P, Staudenmann W, Cook AM, Leisinger T, Kertesz MA: Purification and characterization of the arylsulfatase synthesized by Pseudomonas aeruginosa PAO during growth in sulfate-free medium and clonign of the arylsulfatase gene (atsA). Eur J Biochem 1995, 229:385-394.
41. Kaufman EN, Harkins JB, Borole AP: Comparison of batch-stirred and electrospray reactors for biodesulfurization of dibenzothiophene in crude oil and hydrocarbon feedstocks. Appl Biochem Biotechnol 1998, 73:127-144. This paper identified the ability of Rhodococcus IGTS8 to form very fine emulsions (1-10 μm, average droplet size 2.54 ± 2.40 μm) and to partition into the oil phase during biodesulfurization even in batch reactors, presumably a unique feature of the Rhodococcus and/or its biosurfactant. As a result, the two reactors had almost equal interfacial area. No oxygen mass transport limitation was identified. The authors speculate that the process is limited by the rate of surface renewal as new biocatalyst interacts with the organic-aqueous interface to acquire the dibenzothiophene substrate.
42. Ohshiro T, Hirata T, Hashimoto I, Izumi Y: Characterization of dibenzothiophene desulfurization reaction by whole cells of Rhodococcus erythropolis H-2 in the presence of hydrocarbon. J Ferm Bioeng 1996, 82:610-612.
43. Ohshiro T, Hirata T, Izumi Y: Microbial desulfurization of dibenzothiophene in the presence of hydrocarbon. Appl Microbiol Biotechnol 1995, 44:249-252.
44. Gallardo ME, Ferrandez A, De Lorenzo V, Garcia JL, Diaz E: Designing recombinant Pseudomonas strains to enhance biodesulfurization. J Bacteriol 1997, 179:7156-7160. One of the first reports of the engineering of the Rhodococcus erythropolis IGTS8 dsz genes under the control of heterologous broad-host-range regulatory control to alleviate the mechanism of sulfur repression. The dsz genes were stably inserted into the chromosomes of three different Pseudomonas strains, all of which desulfurized dibenzothiophene more efficiently than the native host Rhodococcus. The largest increase in desulfurization rate (120%) was obtained with a rhamnolipid producing Pseudomonas host. Rhamnolipids are of increasing industrial significance due to their properties with respect to emulsification, wetting, phase separation, and viscosity reduction.
45. Chang JH, Rhee SK, Chank YK, Chang HN: Desulfurization of diesel oils by a newly isolated dibenzothiophene-degrading Nocardia sp. Strain CYKS2. Biotechnol Prog 1998 14:851-855.
46. Premuzic ET, Lin MS: Induced biochemical conversions of heavy crude oils. J Petroleum Sci Eng 1999, 22:171-180.
47. Piddington CS, Kovacevich BR, Rambosek: Sequence and molecular characterization of a DNA region encoding the dibenzothiophene desulfurization operon of Rhodococcus sp. Strain IGTS8. Appl Environ Microbiol 1995, 61:468-475.
48. Denis-Larose C, Bergeron H, Labbe D, Greer CW, Hawari J, Grossman MJ, Sankey BM, Lau PCK: Characterization of the basic replicon of Rhodococcus plasmid pSOX and development of a Rhodococcus-Escherichia coli shuttle vector. Appl Environ Microbiol 1998, 64:4363-4367. A new shuttle plasmid was used to demonstrate expression of the Bacillus subtilis sacB gene in a strain of Rhodococcus rendering it sensitive to sucrose, enabling the use of sucrose sensitivity as a selectable phenotype in screening studies. This new Rhodococcus replicon offers new potential for complementation studies in mycobacteria since the majority of vectors are based on the pAL5000 system.
49. Li MZ, Squires CH, Monticello DJ, Childs JD: Genetic analysis of the dsz promoter and associated regulatory regions of Rhodococcus erythropolis IGTS8. J Bacteriol 1996, 178:6409-6418.
50. Hummerjohann J, Kuttel E, Quadroni M, Ragaller J, Leisinger T, Kertesz MA: Regulation of the sulfate starvation response in Pseudomonas aeruginosa: Role of cysteine biosynthetic intermediates. Microbiology 1998, 144:1375-1386.
51. 2-dependent oxygenase with 22-30% sequence homology to DszA; it catalyzes the desulfonation of alkanesulfonates. The MsuC enzyme had 42% sequence homology with DszC. P. aeruginosa uses methanesulfonate only as a sulfur source, and was unable to utilize dibenzothiophene, methylsulfide, or dimethylsulfide. This system also uses an NADH-dependent FMN reductase (MsuE) required to supply reduced FMN to MsuD.
52. Adams MWW, Kelly RM: Finding and using hyperthermophilic enzymes. Trends Biotechnol 1998, 16:329-332.
53. Robb FT, Maeder DL: Novel evolutionary histories and adaptive features of proteins from hyperthermophiles. Curr Opin Biotechnol 1998, 9:288-291. This paper reviews recent information on proteins from hyperthermophiles, including proteins stable to 200°C, emphasizing enzymes with novel catalytic activity and binding specificities, unprecedented thermal stability and the capacity to stabilize labile metabolites. Industrially useful features of proteins from thermophiles that appear to undergo a stabilizing effect in response to pressure at exceptionally high temperatures are identified. Recent work is discussed that suggests that structural stability of proteins at 100-130°C is maintained by ion-pairing.
54. Inoue A, Horikoshi K: Estimation of solvent-tolerance of bacteria by the solvent parameter log P. J Ferment Bioeng 1991, 71:194-196.
55. de Bont JAM: Solvent-tolerant bacteria in biocatalysis. Trends Biotechnol 1998, 16:493-499.
56. Dordick JS, Khmelnitsky YL, Sergeeva MV: The evolution of biotransformation technologies. Curr Opin Microbiol 1998, 1:311-318. An overview of bioprocessing issues with several good examples, especially for nonaqueous enzyme technology applications and molecular approaches to improving biotransformations.
57. Simon ES, Akiyama A, Whitesides G: Synthesis without cells. In A Revolution in Biotechnology. Edited by Marx JL. Cambridge: Cambridge University Press; 1989:15-27.
58. Ansell RJ, Small DAP, Lowe CR: The interactions of artificial coenzymes with alcohol dehydrogenase and other NAD(P)(H) dependent enzymes. J Molecular Catalysis B:Enzymatic 1999, 6:111-123.
59. Uvarov VY, Shumyantseva VV, Bykhovskaya EA, Kolyada LN, Archakov AI: Semi-artificial hydroxylating enzymes created by flavins binding to cytochrome P450 2b4 and by bleomycin binding to NADPH-cytochrome P450 reductase. Biochem Biophys Res Commun 1994, 200:772-725.
60. Margolin AL: Novel crystalline catalysts. Trends Biotechnol 1996, 14:219-259.
61. 2 advantages. Oil & Gas Journal 1999, Feb:45-48. The economic information presented provides a good starting point for discussion of hydrodesulfurization versus BDS process economic advantages and disadvantages (see also [1•, 11••] for economic information).
62. Mogollon L, Rodriguez R, Larrota W, Ortiz C, Torres R: Biocatalytic removal of nickel and vanadium from petroporphyrins and asphaltenes. Appl Biochem Biotechnol 1998, 70-72:765-777. This paper documents the fractionation of asphaltenes in a heavy crude oil by treatment with chloroperoxidase (cytochrome C peroxidase and lignin peroxidase were ineffective) and the removal of 27 and 53% of the vanadium and nickel, respectively.