메뉴 건너뛰기




Volumn 9, Issue 4, 2011, Pages 478-499

Marine biocatalysts: Enzymatic features and applications

Author keywords

Biocatalysis; Marine biocatalysts; Marine enzymes

Indexed keywords

ALPHA LEVO FUCOSIDASE; AMYLASE; AURANTIIN; LEVOFLOXACIN; OFLOXACIN;

EID: 79955671537     PISSN: None     EISSN: 16603397     Source Type: Journal    
DOI: 10.3390/md9040478     Document Type: Review
Times cited : (190)

References (76)
  • 1
    • 57049092282 scopus 로고    scopus 로고
    • Marine genetic resources: A review of scientific and commercial interest
    • Leary, D.; Vierros, M.; Hamon, G.; Arico, S.; Monagle, C. Marine genetic resources: a review of scientific and commercial interest. Mar. Policy 2009, 33, 183-194.
    • (2009) Mar. Policy , vol.33 , pp. 183-194
    • Leary, D.1    Vierros, M.2    Hamon, G.3    Arico, S.4    Monagle, C.5
  • 2
    • 77955981200 scopus 로고    scopus 로고
    • Potential biocatalysts originating from sea environments
    • Trincone, A. Potential biocatalysts originating from sea environments. J. Mol. Catal. B Enzym. 2010, 66, 241-256.
    • (2010) J. Mol. Catal. B Enzym. , vol.66 , pp. 241-256
    • Trincone, A.1
  • 4
    • 27844612307 scopus 로고    scopus 로고
    • Extreme environments as a resource for microorganisms and novel biocatalysts
    • DOI 10.1007/b135786, Marine Biotechnology I
    • Antranikian, G.; Vorgias, C.E.; Bertoldo, C. Extreme environments as a resource for microorganisms and novel biocatalysts. Adv. Biochem. Eng. Biotechnol. 2005, 96, 219-262. (Pubitemid 44617135)
    • (2005) Advances in Biochemical Engineering/Biotechnology , vol.96 , pp. 219-262
    • Antranikian, G.1    Vorgias, C.E.2    Bertoldo, C.3
  • 7
    • 65549091127 scopus 로고    scopus 로고
    • Marine biominerals: Perspectives and challenges for polymetallic nodules and crusts
    • Wang, X.; Müller, W.E.G. Marine biominerals: perspectives and challenges for polymetallic nodules and crusts. Trends Biotechnol. 2009, 27, 375-383.
    • (2009) Trends Biotechnol. , vol.27 , pp. 375-383
    • Wang, X.1    Müller, W.E.G.2
  • 8
    • 84889381937 scopus 로고    scopus 로고
    • Conversion of fisheries by-products and waste into value-added products-Attempts undergoing in Hokkaido, Japan
    • Hou, C.T., Shaw, J.-F., Eds.; John Wiley and Sons: Hoboken, NJ, USA
    • Takahashi, K.; Fukunaga, K. Conversion of fisheries by-products and waste into value-added products-Attempts undergoing in Hokkaido, Japan. In Biocatalysis and Bioenergy; Hou, C.T., Shaw, J.-F., Eds.; John Wiley and Sons: Hoboken, NJ, USA, 2008; pp. 417-430.
    • (2008) Biocatalysis and Bioenergy , pp. 417-430
    • Takahashi, K.1    Fukunaga, K.2
  • 9
    • 0037290663 scopus 로고    scopus 로고
    • Fish bioaccumulation and biomarkers in environmental risk assessment: A review
    • DOI 10.1016/S1382-6689(02)00126-6, PII S1382668902001266
    • van der Oost, R.; Beyer, J.; Vermeulen, N.P.E. Fish bioaccumulation and biomarkers in environmental risk assessment: a review. Environ. Toxicol. Pharmacol. 2003, 13, 57-149. (Pubitemid 35441240)
    • (2003) Environmental Toxicology and Pharmacology , vol.13 , Issue.2 , pp. 57-149
    • Van Der, O.R.1    Beyer, J.2    Vermeulen, N.P.E.3
  • 10
    • 38749110083 scopus 로고    scopus 로고
    • Biotransformation of polycyclic aromatic hydrocarbons in marine polychaetes
    • DOI 10.1016/j.marenvres.2007.10.001, PII S0141113607001274
    • Jorgensen, A.; Giessing, A.M.B.; Rasmussen, L.J.; Andersen, O. Biotransformation of polycyclic aromatic hydrocarbons in marine polychaetes. Mar. Environ. Res. 2008, 65, 171-186. (Pubitemid 351178768)
    • (2008) Marine Environmental Research , vol.65 , Issue.2 , pp. 171-186
    • Jorgensen, A.1    Giessing, A.M.B.2    Rasmussen, L.J.3    Andersen, O.4
  • 12
    • 33745460366 scopus 로고    scopus 로고
    • Molecular Biomarkers: Their significance and application in marine pollution monitoring
    • DOI 10.1007/s10646-006-0069-1
    • Sarkar, A.; Ray, D.; Shrivastava, A.N.; Sarker, S. Molecular biomarkers: their significance and application in marine pollution monitoring. Ecotoxicology 2006, 15, 333-340. (Pubitemid 43954045)
    • (2006) Ecotoxicology , vol.15 , Issue.4 , pp. 333-340
    • Sarkar, A.1    Ray, D.2    Shrivastava, A.N.3    Sarker, S.4
  • 13
    • 33746308468 scopus 로고    scopus 로고
    • Identification of proteomic signatures of exposure to marine pollutants in mussels (Mytilus edulis)
    • DOI 10.1074/mcp.M500333-MCP200
    • Apraiz, I.; Cristobal, S. Identification of proteomic signatures of exposure to marine pollutants in mussels (Mytilus edulis). Mol. Cell. Proteomics 2006, 5, 1274-1285. (Pubitemid 44103398)
    • (2006) Molecular and Cellular Proteomics , vol.5 , Issue.7 , pp. 1274-1285
    • Apraiz, I.1    Mi, J.2    Cristobal, S.3
  • 15
    • 77955982960 scopus 로고    scopus 로고
    • Novel molecular methods for discovery and enginnering of biocatalysts from uncultured marine microorganisms
    • Uria, A.R.; Fawzya, Y.N.; Chasanah, E. Novel molecular methods for discovery and enginnering of biocatalysts from uncultured marine microorganisms. J. Coast. Dev. 2005, 8, 53-71.
    • (2005) J. Coast. Dev. , vol.8 , pp. 53-71
    • Uria, A.R.1    Fawzya, Y.N.2    Chasanah, E.3
  • 16
    • 52449101850 scopus 로고    scopus 로고
    • Marine metagenomics: Strategies for the discovery of novel enzymes with biotechnological applications from marine environments
    • Kennedy, J.; Marchesi, J.R.; Dobson, A.D.W. Marine metagenomics: strategies for the discovery of novel enzymes with biotechnological applications from marine environments. Microb. Cell Fact. 2008, 7, 27-34.
    • (2008) Microb. Cell Fact. , vol.7 , pp. 27-34
    • Kennedy, J.1    Marchesi, J.R.2    Dobson, A.D.W.3
  • 17
    • 70350736731 scopus 로고    scopus 로고
    • Polyketide synthases of bacterial symbionts in sponges-Evolution-based applications in natural products research
    • Hochmuth, T.; Piel, J. Polyketide synthases of bacterial symbionts in sponges-Evolution-based applications in natural products research. Phytochemistry 2009, 70, 1841-1849.
    • (2009) Phytochemistry , vol.70 , pp. 1841-1849
    • Hochmuth, T.1    Piel, J.2
  • 20
    • 77952487092 scopus 로고    scopus 로고
    • Finding new enzymes from bacterial physiology: A successful approach illustrated by the detection of novel oxidases in Marinomonas mediterranea
    • Sanchez-Amat, A.; Solano, F.; Lucas-Elío, P. Finding new enzymes from bacterial physiology: a successful approach illustrated by the detection of novel oxidases in Marinomonas mediterranea. Mar. Drugs 2010, 8, 519-541.
    • (2010) Mar. Drugs , vol.8 , pp. 519-541
    • Sanchez-Amat, A.1    Solano, F.2    Lucas-Elío, P.3
  • 21
    • 77952571563 scopus 로고    scopus 로고
    • Bioprocessing data for the production of marine enzymes
    • Sarkar, S.; Pramanik, A.; Mitra, A.; Mukherjee, J. Bioprocessing data for the production of marine enzymes. Mar. Drugs 2010, 8, 1323-1372.
    • (2010) Mar. Drugs , vol.8 , pp. 1323-1372
    • Sarkar, S.1    Pramanik, A.2    Mitra, A.3    Mukherjee, J.4
  • 23
    • 76849099236 scopus 로고    scopus 로고
    • Synthesis and production of polyhydroxyalkanoates by halophiles: Current potential and future prospects
    • Quillaguamán, J.; Guzmán, H.; Van-Thuoc, D.; Hatti-Kaul R. Synthesis and production of polyhydroxyalkanoates by halophiles: current potential and future prospects. Appl. Microbiol. Biotechnol. 2010, 85, 1687-1696.
    • (2010) Appl. Microbiol. Biotechnol. , vol.85 , pp. 1687-1696
    • Quillaguamán, J.1    Guzmán, H.2    Van-Thuoc, D.3    Hatti-Kaul, R.4
  • 24
    • 0036669804 scopus 로고    scopus 로고
    • Extreme halophilic enzymes in organic solvents
    • DOI 10.1016/S0958-1669(02)00338-5
    • Marhuenda-Egea, F.C.; Bonete, M.J. Extreme halophilic enzymes in organic solvents. Curr. Opin. Biotechnol. 2002, 13, 385-389. (Pubitemid 35254098)
    • (2002) Current Opinion in Biotechnology , vol.13 , Issue.4 , pp. 385-389
    • Marhuenda-Egea, F.C.1    Bonete, M.J.2
  • 25
    • 0036549657 scopus 로고    scopus 로고
    • Extremely thermostable glutamate dehydrogenase (GDH) from the freshwater archaeon Thermococcus waiotapuensis: Cloning and comparison with two marine hyperthermophilic GDHs
    • DOI 10.1007/s007920100238
    • Lee, M.-K.; González, J.M.; Robb, F.T. Extremely thermostable glutamate dehydrogenase (GDH) from the freshwater archaeon Thermococcus waiotapuensis: cloning and comparison with two marine hyperthermophilic GDHs. Extremophiles 2002, 6, 151-159. (Pubitemid 41490483)
    • (2002) Extremophiles , vol.6 , Issue.2 , pp. 151-159
    • Lee, M.-K.1    Gonzalez, J.M.2    Robb, F.T.3
  • 28
    • 77952140013 scopus 로고    scopus 로고
    • Biochemical properties of anionic trypsin acting at high concentration of NaCl purified from the intestine of a carnivorous fish: Smooth hound (Mustelus mustelus)
    • Bougatef, A.; Balti, R.; Nasri, R.; Jellouli, K.; Soussi, N.; Nasri, M. Biochemical properties of anionic trypsin acting at high concentration of NaCl purified from the intestine of a carnivorous fish: smooth hound (Mustelus mustelus). J. Agric. Food Chem. 2010, 58, 5763-5769.
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 5763-5769
    • Bougatef, A.1    Balti, R.2    Nasri, R.3    Jellouli, K.4    Soussi, N.5    Nasri, M.6
  • 29
    • 0035961604 scopus 로고    scopus 로고
    • Purification and characterization of alanine racemase from hepatopancreas of black-tiger prawn, Penaeus monodon
    • Uo, T.; Ueda, M.; Nishiyama, T.; Yoshimura, T.; Esaki, N. Purification and characterization of alanine racemase from hepatopancreas of black-tiger prawn, Penaeus monodon. J. Mol. Catal. B Enzym. 2001, 12, 137-144.
    • (2001) J. Mol. Catal. B Enzym. , vol.12 , pp. 137-144
    • Uo, T.1    Ueda, M.2    Nishiyama, T.3    Yoshimura, T.4    Esaki, N.5
  • 30
    • 27844584367 scopus 로고    scopus 로고
    • Industrial relevance of thermophilic Archaea
    • DOI 10.1016/j.mib.2005.10.015, PII S1369527405001712, Growth Development
    • Egorova, K.; Antranikian, G. Industrial relevance of thermophilic Archaea. Curr. Opin. Microbiol. 2005, 8, 649-655. (Pubitemid 41643962)
    • (2005) Current Opinion in Microbiology , vol.8 , Issue.6 , pp. 649-655
    • Egorova, K.1    Antranikian, G.2
  • 31
    • 65349190562 scopus 로고    scopus 로고
    • Recent progress in biocatalysis for asymmetric oxidation and reduction
    • Matsuda, T.; Nakamura, K. Recent progress in biocatalysis for asymmetric oxidation and reduction. Tetrahedron Asymmetry 2009, 20, 513-557.
    • (2009) Tetrahedron Asymmetry , vol.20 , pp. 513-557
    • Matsuda, T.1    Nakamura, K.2
  • 32
    • 33845205018 scopus 로고    scopus 로고
    • Asymmetric ketone reduction by a hyperthermophilic alcohol dehydrogenase. The substrate specificity, enantioselectivity and tolerance of organic solvents
    • DOI 10.1016/j.tetasy.2006.10.042, PII S0957416606007907
    • Zhu, D.; Malik, H.T.; Hua, L. Asymmetric ketone reduction by a hyperthermophilic alcohol dehydrogenase. The substrate specificity, enantioselectivity and tolerance of organic solvents. Tetrahedron Asymmetry 2006, 17, 3010-3014. (Pubitemid 44855545)
    • (2006) Tetrahedron Asymmetry , vol.17 , Issue.21 , pp. 3010-3014
    • Zhu, D.1    Malik, H.T.2    Hua, L.3
  • 33
    • 0035965060 scopus 로고    scopus 로고
    • Characterization of a thermostable β-glucosidase (BglB) from Thermotoga maritima showing transglycosylation activity
    • DOI 10.1016/S1381-1177(01)00003-0, PII S1381117701000030
    • Goyal, K.; Selvakumar, P.; Hayashi, K. Characterization of a thermostable β-glucosidase (BglB) from Thermotoga maritima showing transglycosylation activity. J. Mol. Catal. B Enzym. 2001, 15, 45-53. (Pubitemid 32768680)
    • (2001) Journal of Molecular Catalysis - B Enzymatic , vol.15 , Issue.1-3 , pp. 45-53
    • Goyal, K.1    Selvakumar, P.2    Hayashi, K.3
  • 34
    • 1242315605 scopus 로고    scopus 로고
    • The recombinant xylanase B of Thermotoga maritima is highly xylan specific and produces exclusively xylobiose from xylans, a unique character for industrial applications
    • DOI 10.1016/j.molcatb.2003.11.012
    • Jiang, Z.Q.; Deng, W.; Zhu, Y.P.; Li, L.T.; Sheng, Y.J.; Hayashi, K. The recombinant xylanase B of Thermotoga maritima is highly xylan specific and produces exclusively xylobiose from xylans, a unique character for industrial applications. J. Mol. Catal. B Enzym. 2004, 27, 207-213. (Pubitemid 38221108)
    • (2004) Journal of Molecular Catalysis B: Enzymatic , vol.27 , Issue.4-6 , pp. 207-213
    • Jiang, Z.Q.1    Deng, W.2    Zhu, Y.P.3    Li, L.T.4    Sheng, Y.J.5    Hayashi, K.6
  • 35
    • 34249333446 scopus 로고    scopus 로고
    • Transglycosylation reactions using glycosyl hydrolases from Thermotoga neapolitana, a marine hydrogen-producing bacterium
    • DOI 10.1016/j.molcatb.2007.03.005, PII S1381117707000641
    • Tramice, A.; Pagnotta, E.; Romano, I.; Gambacorta, A.; Trincone, A. Transglycosylation reactions using glycosyl hydrolases from Thermotoga neapolitana, a marine hydrogen-producing bacterium. J. Mol. Catal. B Enzym. 2007, 47, 21-27. (Pubitemid 46819150)
    • (2007) Journal of Molecular Catalysis B: Enzymatic , vol.47 , Issue.1-2 , pp. 21-27
    • Tramice, A.1    Pagnotta, E.2    Romano, I.3    Gambacorta, A.4    Trincone, A.5
  • 37
    • 0026956057 scopus 로고
    • Microbial life at high pressures
    • Bartlett, D.H. Microbial life at high pressures. Sci. Prog. (Oxf.) 1992, 76, 479-496.
    • (1992) Sci. Prog. (Oxf.) , vol.76 , pp. 479-496
    • Bartlett, D.H.1
  • 38
    • 0035283618 scopus 로고    scopus 로고
    • The biotechnological potential of piezophiles
    • DOI 10.1016/S0167-7799(00)01539-0, PII S0167779900015390
    • Abe, F.; Horikoshi, K. The biotechnological potential of piezophiles. Trends Biotechnol. 2001, 19, 102-108. (Pubitemid 32155430)
    • (2001) Trends in Biotechnology , vol.19 , Issue.3 , pp. 102-108
    • Abe, F.1    Horikoshi, K.2
  • 39
    • 0032082973 scopus 로고    scopus 로고
    • Barophiles: Deep-sea microorganisms adapted to an extreme environment
    • Horikoshi, K. Barophiles: deep-sea microorganisms adapted to an extreme environment. Curr. Opin. Microbiol. 1998, 1, 291-295.
    • (1998) Curr. Opin. Microbiol. , vol.1 , pp. 291-295
    • Horikoshi, K.1
  • 41
    • 0030839133 scopus 로고    scopus 로고
    • Pressure and temperature effects on growth and viability of the hyperthermophilic archaeon Thermococcus peptonophilus
    • Canganella, F.; Gonzalez, J.M.; Yanagibayashi, M.; Kato, C.; Horikoshi, K. Pressure and temperature effects on growth and viability of the hyperthermophilic archaeon Thermococcus peptonophilus. Arch. Microbiol. 1997, 168, 1-7.
    • (1997) Arch. Microbiol. , vol.168 , pp. 1-7
    • Canganella, F.1    Gonzalez, J.M.2    Yanagibayashi, M.3    Kato, C.4    Horikoshi, K.5
  • 42
    • 0027945986 scopus 로고
    • New method for isolating barophiles from intestinal contents of deep-sea fishes retrieved from the abyssal zone
    • Nakayama, A.; Yano, Y.; Yoshida, K. New method for the isolation of barophiles from intestinal contents of deep-sea fishes retrieved from the abyssal zone. Appl. Environ. Microbiol. 1994, 60, 4210-4212. (Pubitemid 24335889)
    • (1994) Applied and Environmental Microbiology , vol.60 , Issue.11 , pp. 4210-4212
    • Nakayama, A.1    Yano, Y.2    Yoshida, K.3
  • 43
    • 1842664387 scopus 로고    scopus 로고
    • Biosynthesis and dietary uptake of polyunsaturated fatty acids by piezophilic bacteria
    • Fang, J.; Kato, C.; Sato, T.; Chan, O.; McKay, D. Biosynthesis and dietary uptake of polyunsaturated fatty acids by piezophilic bacteria. Comp. Biochem. Physiol. B 2004, 137, 455-461.
    • (2004) Comp. Biochem. Physiol. B , vol.137 , pp. 455-461
    • Fang, J.1    Kato, C.2    Sato, T.3    Chan, O.4    McKay, D.5
  • 44
    • 33749046141 scopus 로고    scopus 로고
    • Origins of life and biochemistry under high-pressure conditions
    • DOI 10.1039/b517766a
    • Daniel, I.; Oger, P.; Winter, R. Origins of life and biochemistry under high-pressure conditions. Chem. Soc. Rev. 2006, 35, 858-875. (Pubitemid 44465572)
    • (2006) Chemical Society Reviews , vol.35 , Issue.10 , pp. 858-875
    • Daniel, I.1    Oger, P.2    Winter, R.3
  • 45
    • 33750040235 scopus 로고    scopus 로고
    • Lipolytic activity of Antarctic cold-adapted marine bacteria (Terra Nova Bay, Ross Sea)
    • DOI 10.1111/j.1365-2672.2006.03006.x
    • Lo Giudice, A.; Michaud, L.; de Pascale, D.; De Domenico, M.; di Prisco, G.; Fani, R.; Bruni, V. Lipolytic activity of Antarctic cold-adapted marine bacteria (Terra Nova Bay, Ross Sea). J. Appl. Microbiol. 2006, 101, 1039-1048. (Pubitemid 44581895)
    • (2006) Journal of Applied Microbiology , vol.101 , Issue.5 , pp. 1039-1048
    • Lo, G.A.1    Michaud, L.2    De Pascale, D.3    De Domenico, M.4    Di, P.G.5    Fani, R.6    Bruni, V.7
  • 47
    • 70349758093 scopus 로고    scopus 로고
    • Characterization of inducible cold-active β-glucosidases from the psychrotolerant bacterium Shewanella sp. G5 isolated from a sub-Antarctic ecosystem
    • Cristóbal, H.A.; Schmidt, A.; Kothe, E.; Breccia, J.; Abate, C.M. Characterization of inducible cold-active β-glucosidases from the psychrotolerant bacterium Shewanella sp. G5 isolated from a sub-Antarctic ecosystem. Enzym. Microb. Technol. 2009, 45, 498-506.
    • (2009) Enzym. Microb. Technol. , vol.45 , pp. 498-506
    • Cristóbal, H.A.1    Schmidt, A.2    Kothe, E.3    Breccia, J.4    Abate, C.M.5
  • 48
    • 77951768870 scopus 로고    scopus 로고
    • A cold-adapted esterase of a novel marine isolate, Pseudoalteromonas arctica: Gene cloning, enzyme purification and characterization
    • Khudary, R.A.; Venkatachalam, R.; Katzer, M.; Elleuche, S.; Antranikian, G. A cold-adapted esterase of a novel marine isolate, Pseudoalteromonas arctica: gene cloning, enzyme purification and characterization. Extremophiles 2010, 14, 273-285.
    • (2010) Extremophiles , vol.14 , pp. 273-285
    • Khudary, R.A.1    Venkatachalam, R.2    Katzer, M.3    Elleuche, S.4    Antranikian, G.5
  • 49
    • 36649004271 scopus 로고    scopus 로고
    • Biosynthesis of (R)-phenyl-1,2-ethanediol from racemic styrene oxide by using bacterial and marine fish epoxide hydrolases
    • DOI 10.1007/s10529-007-9495-2
    • Kim, H.S.; Lee, O.K.; Hwang, S.; Kim, B.J.; Lee, E.Y. Biosynthesis of (R)-phenyl-1,2-ethanediol from racemic styrene oxide by using bacterial and marine fish epoxide hydrolases. Biotechnol. Lett. 2008, 30, 127-133. (Pubitemid 350197794)
    • (2008) Biotechnology Letters , vol.30 , Issue.1 , pp. 127-133
    • Kim, H.S.1    Lee, O.K.2    Hwang, S.3    Kim, B.J.4    Lee, E.Y.5
  • 50
    • 33746353988 scopus 로고    scopus 로고
    • Enantioselective epoxide hydrolase activity of a newly isolated microorganism, Sphingomonas echinoides EH-983, from seawater
    • DOI 10.1016/j.molcatb.2006.05.009, PII S1381117706001688
    • Kim, H.S.; Lee, O.K.; Lee, S.J.; Hwang, S.; Kim, S.J.; Yang, S.H.; Park, S.; Lee, E.Y. Enantioselective epoxide hydrolase activity of a newly isolated microorganism, Sphingomonas echinoides EH-983, from seawater. J. Mol. Catal. B Enzym. 2006, 41, 130-135. (Pubitemid 44118815)
    • (2006) Journal of Molecular Catalysis B: Enzymatic , vol.41 , Issue.3-4 , pp. 130-135
    • Kim, H.S.1    Lee, O.K.2    Lee, S.J.3    Hwang, S.4    Kim, S.J.5    Yang, S.-H.6    Park, S.7    Lee, E.Y.8
  • 51
    • 27944452636 scopus 로고    scopus 로고
    • Cloning and characterization of a fish microsomal epoxide hydrolase of Danio rerio and application to kinetic resolution of racemic styrene oxide
    • Kim, H.S.; Lee, S.J.; Lee, E.J.; Hwang, J.W.; Park, S.; Kim, S.J.; Lee, E.Y. Cloning and characterization of a fish microsomal epoxide hydrolase of Danio rerio and application to kinetic resolution of racemic styrene oxide. J. Mol. Catal. B Enzym. 2005, 37, 30-35.
    • (2005) J. Mol. Catal. B Enzym. , vol.37 , pp. 30-35
    • Kim, H.S.1    Lee, S.J.2    Lee, E.J.3    Hwang, J.W.4    Park, S.5    Kim, S.J.6    Lee, E.Y.7
  • 52
    • 77952108311 scopus 로고    scopus 로고
    • Biocatalytic resolution of glycidyl phenyl ether using a novel epoxide hydrolase from a marine bacterium, Rhodobacterales bacterium HTCC2654
    • Woo, J.-H.; Kang, J.-H.; Hwang, Y.-O.; Cho, J.-C.; Kim, S.-J.; Kang, S.G. Biocatalytic resolution of glycidyl phenyl ether using a novel epoxide hydrolase from a marine bacterium, Rhodobacterales bacterium HTCC2654. J. Biosci. Bioeng. 2010, 109, 539-544.
    • (2010) J. Biosci. Bioeng. , vol.109 , pp. 539-544
    • Woo, J.-H.1    Kang, J.-H.2    Hwang, Y.-O.3    Cho, J.-C.4    Kim, S.-J.5    Kang, S.G.6
  • 53
    • 38749110083 scopus 로고    scopus 로고
    • Biotransformation of polycyclic aromatic hydrocarbons in marine polychaetes
    • DOI 10.1016/j.marenvres.2007.10.001, PII S0141113607001274
    • Jorgensen, A.; Giessing, A.M.B.; Rasmussen, L.J.; Andersen, O. Biotransformation of polycyclic aromatic hydrocarbons in marine polychaetes. Mar. Environ. Res. 2008, 65, 171-186. (Pubitemid 351178768)
    • (2008) Marine Environmental Research , vol.65 , Issue.2 , pp. 171-186
    • Jorgensen, A.1    Giessing, A.M.B.2    Rasmussen, L.J.3    Andersen, O.4
  • 54
    • 34547790929 scopus 로고    scopus 로고
    • Hydroxylations of substituted naphthalenes by Escherichia coli expressing aromatic dihydroxylating dioxygenase genes from polycyclic aromatic hydrocarbon-utilizing marine bacteria
    • DOI 10.1016/j.molcatb.2007.06.007, PII S138111770700118X
    • Shindo, K.; Osawa, A.; Kasai, Y.; Iba, N.; Saotome, A.; Misawa, N. Hydroxylations of substituted naphthalenes by Escherichia coli expressing aromatic dihydroxylating dioxygenase genes from polycyclic aromatic hydrocarbon-utilizing marine bacteria. J. Mol. Catal. B Enzym. 2007, 48, 77-83. (Pubitemid 47239485)
    • (2007) Journal of Molecular Catalysis B: Enzymatic , vol.48 , Issue.3-4 , pp. 77-83
    • Shindo, K.1    Osawa, A.2    Kasai, Y.3    Iba, N.4    Saotome, A.5    Misawa, N.6
  • 55
    • 72949106034 scopus 로고    scopus 로고
    • Novel alkane hydroxylase (alkB) gene diversity in sediments associated with hydrocarbon seeps in the Timor Sea, Australia
    • Wasmund, K.; Burns, K.A.; Kurtboke, D.I.; Boume, D.G. Novel alkane hydroxylase (alkB) gene diversity in sediments associated with hydrocarbon seeps in the Timor Sea, Australia. Appl. Environ. Microbiol. 2009, 75, 7391-7398.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 7391-7398
    • Wasmund, K.1    Burns, K.A.2    Kurtboke, D.I.3    Boume, D.G.4
  • 56
    • 77951765709 scopus 로고    scopus 로고
    • Production of a recombinant alkane hydroxylase (AlkB2) from Alcanivorax borkumensis
    • Miri, M.; Bambai, B.; Tabandeh, F.; Sadeghizadeh, M.; Kamali, N. Production of a recombinant alkane hydroxylase (AlkB2) from Alcanivorax borkumensis. Biotechnol. Lett. 2010, 32, 497-502.
    • (2010) Biotechnol. Lett. , vol.32 , pp. 497-502
    • Miri, M.1    Bambai, B.2    Tabandeh, F.3    Sadeghizadeh, M.4    Kamali, N.5
  • 57
    • 2342586601 scopus 로고    scopus 로고
    • Transglycosylation reactions performed by glycosyl hydrolases from the marine anaspidean mollusc Aplysia fasciata
    • DOI 10.1016/j.molcatb.2004.03.007, PII S1381117704001134
    • Giordano, A.; Andreotti, G.; Mollo, E.; Trincone, A. Transglycosylation reactions performed by glycosyl hydrolases from the marine anaspidean mollusc Aplysia fasciata. J. Mol. Catal. B Enzym. 2004, 30, 51-59. (Pubitemid 38597101)
    • (2004) Journal of Molecular Catalysis B: Enzymatic , vol.30 , Issue.2 , pp. 51-59
    • Giordano, A.1    Andreotti, G.2    Mollo, E.3    Trincone, A.4
  • 58
    • 23444442392 scopus 로고    scopus 로고
    • Purification and characterization of a β-D-mannosidase from the marine anaspidean Aplysia fasciata
    • Andreotti, G.; Giordano, A.; Tramice, A.; Mollo, E.; Trincone, A. Purification and characterization of a β-D-mannosidase from the marine anaspidean Aplysia fasciata. J. Biotechnol. 2005, 119, 26-35.
    • (2005) J. Biotechnol. , vol.119 , pp. 26-35
    • Andreotti, G.1    Giordano, A.2    Tramice, A.3    Mollo, E.4    Trincone, A.5
  • 59
    • 33644510085 scopus 로고    scopus 로고
    • Hydrolyses and transglycosylations performed by purified α-D-glucosidase of the marine mollusc Aplysia fasciata
    • Andreotti, G.; Giordano, A.; Tramice, A.; Mollo, E.; Trincone, A. Hydrolyses and transglycosylations performed by purified α-D-glucosidase of the marine mollusc Aplysia fasciata. J. Biotechnol. 2006, 122, 274-284.
    • (2006) J. Biotechnol. , vol.122 , pp. 274-284
    • Andreotti, G.1    Giordano, A.2    Tramice, A.3    Mollo, E.4    Trincone, A.5
  • 60
    • 9644263987 scopus 로고    scopus 로고
    • Enzymatic syntheses and selective hydrolysis of O-β-d- galactopyranosides using a marine mollusc β-galactosidase
    • DOI 10.1016/j.bmcl.2004.10.016, PII S0960894X04012442
    • Giordano, A.; Tramice, A.; Andreotti, G.; Mollo, E.; Trincone, A. Enzymatic syntheses and selective hydrolysis of O-β-D-galactopyranosides using a marine mollusc β-galactosidase. Bioorg. Med. Chem. Lett. 2005, 15, 139-143. (Pubitemid 39575799)
    • (2005) Bioorganic and Medicinal Chemistry Letters , vol.15 , Issue.1 , pp. 139-143
    • Giordano, A.1    Tramice, A.2    Andreotti, G.3    Mollo, E.4    Trincone, A.5
  • 61
    • 34249275684 scopus 로고    scopus 로고
    • Convenient synthesis of β-galactosyl nucleosides using the marine β-galactosidase from Aplysia fasciata
    • DOI 10.1016/j.molcatb.2007.03.006, PII S1381117707000665
    • Andreotti, G.; Trincone, A.; Giordano, A. Convenient synthesis of β-galactosyl nucleosides using the marine β-galactosidase from Aplysia fasciata. J. Mol. Catal. B Enzym. 2007, 47, 28-32. (Pubitemid 46819152)
    • (2007) Journal of Molecular Catalysis B: Enzymatic , vol.47 , Issue.1-2 , pp. 28-32
    • Andreotti, G.1    Trincone, A.2    Giordano, A.3
  • 62
    • 33750530819 scopus 로고    scopus 로고
    • High-yielding enzymatic α-glucosylation of pyridoxine by marine α-glucosidase from Aplysia fasciata
    • DOI 10.1007/s10126-005-6144-4
    • Tramice, A.; Andreotti, G.; Trincone, A. High-yielding enzymatic α-glucosylation of pyridoxine by marine α-glucosidase from Aplysia fasciata. Mar. Biotechnol. 2006, 8, 448-452. (Pubitemid 44663642)
    • (2006) Marine Biotechnology , vol.8 , Issue.5 , pp. 448-452
    • Tramice, A.1    Giordano, A.2    Andreotti, G.3    Mollo, E.4    Trincone, A.5
  • 63
    • 42949127643 scopus 로고    scopus 로고
    • Direct enzymatic glucosylation of naringin in grapefruit juice by α-D-glucosidase from the marine mollusc Aplysia fasciata
    • DOI 10.1002/biot.200700161
    • Tramice, A.; Andreotti, G.; Trincone, A. Direct enzymatic glucosylation of naringin in grapefruit juice by α-D-glucosidase from the marine mollusc Aplysia fasciata. Biotechnol. J. 2008, 3, 545-554. (Pubitemid 351618740)
    • (2008) Biotechnology Journal , vol.3 , Issue.4 , pp. 545-554
    • Tramice, A.1    Andreotti, G.2    Trincone, A.3
  • 66
    • 0036019906 scopus 로고    scopus 로고
    • Characterization of a new α-L-fucosidase isolated from the marine mollusk Pecten maximus that catalyzes the hydrolysis of α-L-fucose from algal fucoidan (Ascophyllum nodosum)
    • Berteau, O.; McCort, I.; Goasdonuè, N.; Tissot, B.; Daniel, R. Characterization of a new α-L-fucosidase isolated from the marine mollusk Pecten maximus that catalyzes the hydrolysis of α-L-fucose from algal fucoidan (Ascophyllum nodosum). Glycobiology 2002, 4, 273-282. (Pubitemid 34760072)
    • (2002) Glycobiology , vol.12 , Issue.4 , pp. 273-282
    • Berteau, O.1    McCort, I.2    Goasdoue, N.3    Tissot, B.4    Daniel, R.5
  • 67
    • 2942741170 scopus 로고    scopus 로고
    • α-L-Fucosidases: Exoglycosidases with unusual transglycosylation properties
    • DOI 10.1021/bi036066z
    • Berteau, O.; Bielicki, J.; Kilonda, A.; Machy, D.; Anson, D.S.; Kenne, L. α-L-Fucosidases: exoglycosidases with unusual transglycosylation properties. Biochemistry 2004, 22, 7881-7891. (Pubitemid 38787697)
    • (2004) Biochemistry , vol.43 , Issue.24 , pp. 7881-7891
    • Berteau, O.1    Bielicki, J.2    Kilonda, A.3    Machy, D.4    Anson, D.S.5    Kenne, L.6
  • 68
    • 35148893576 scopus 로고    scopus 로고
    • Enzymatic synthesis of polyglucosylfructosides from sucrose alone by a novel α-glucosidase isolated from the digestive juice of Archachatina ventricosa (Achatinideae)
    • DOI 10.1016/j.enzmictec.2007.07.024, PII S0141022907002670
    • Soro, R.Y.; Diopoh, J.K.; Willemot, R.-M.; Combes, D. Enzymatic synthesis of polyglucosylfructosides from sucrose alone by a novel α-glucosidase isolated from the digestive juice of Archachatina ventricosa (Achatinideae). Enzym. Microb. Technol. 2007, 42, 44-51. (Pubitemid 47538736)
    • (2007) Enzyme and Microbial Technology , vol.42 , Issue.1 , pp. 44-51
    • Soro, R.Y.1    Diopoh, J.K.2    Willemot, R.-M.3    Combes, D.4
  • 69
    • 76149105468 scopus 로고    scopus 로고
    • A novel β-Agarase with high pH stability from marine Agarivorans sp. LQ48
    • Long, M.; Yu, Z.; Xu, X. A novel β-Agarase with high pH stability from marine Agarivorans sp. LQ48. Mar. Biotechnol. 2010, 12, 62-69.
    • (2010) Mar. Biotechnol. , vol.12 , pp. 62-69
    • Long, M.1    Yu, Z.2    Xu, X.3
  • 71
    • 70349096860 scopus 로고    scopus 로고
    • A unique β-1,2-mannosyltransferase of Thermotoga maritima that uses di-myo-inositol phosphate as the mannosyl acceptor
    • Rodrigues, M.V.; Borges, N.; Almeida, C.P.; Lamosa, P.; Santos, H. A unique β-1,2-mannosyltransferase of Thermotoga maritima that uses di-myo-inositol phosphate as the mannosyl acceptor. J. Bacteriol. 2009, 191, 6105-6115.
    • (2009) J. Bacteriol. , vol.191 , pp. 6105-6115
    • Rodrigues, M.V.1    Borges, N.2    Almeida, C.P.3    Lamosa, P.4    Santos, H.5
  • 72
    • 33847265370 scopus 로고    scopus 로고
    • Screening and its potential application of lipolytic activity from a marine environment: Characterization of a novel esterase from Yarrowia lipolytica CL180
    • Kim, J.-T; Kang, S.G.; Woo, J.-H.; Lee, J.-H.; Jeong, B.C.; Kim, S.-J. Screening and its potential application of lipolytic activity from a marine environment: characterization of a novel esterase from Yarrowia lipolytica CL180. Appl. Microbiol. Biotechnol. 2007, 74, 820-828.
    • (2007) Appl. Microbiol. Biotechnol. , vol.74 , pp. 820-828
    • Kim, J.-T.1    Kang, S.G.2    Woo, J.-H.3    Lee, J.-H.4    Jeong, B.C.5    Kim, S.-J.6
  • 73
    • 67749142086 scopus 로고    scopus 로고
    • Using marine natural products to discover a protease that catalyzes peptide macrocyclization of diverse substrates
    • Lee, J.; McIntosh, J.; Hathaway, B.J.; Schmidt, E.W. Using marine natural products to discover a protease that catalyzes peptide macrocyclization of diverse substrates. J. Am. Chem. Soc. 2009, 131, 2122-2124.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 2122-2124
    • Lee, J.1    McIntosh, J.2    Hathaway, B.J.3    Schmidt, E.W.4
  • 74
    • 0036335795 scopus 로고    scopus 로고
    • Enantioselective formation of (R)-9-HPODE and (R)-9-HPOTrE in marine green alga Ulva conglobata
    • DOI 10.1016/S0968-0896(02)00212-2, PII S0968089602002122
    • Akakabe, Y.; Matsui, K.; Kajiwara, T. Enantioselective formation of (R)-9-HPODE and (R)-9-HPOTrE in marine green alga Ulva conglobata. Bioorg. Med. Chem. Lett. 2002, 10, 3171-3173. (Pubitemid 34855390)
    • (2002) Bioorganic and Medicinal Chemistry , vol.10 , Issue.10 , pp. 3171-3173
    • Akakabe, Y.1    Matsui, K.2    Kajiwara, T.3
  • 76
    • 79955670877 scopus 로고    scopus 로고
    • Steroid catabolism in marine and freshwater fish
    • doi:10.1016/j.jsbmb.2010.10.003
    • James, M.O. Steroid catabolism in marine and freshwater fish. J. Steroid Biochem. Mol. Biol. 2010, doi:10.1016/j.jsbmb.2010.10.003.
    • (2010) J. Steroid Biochem. Mol. Biol.
    • James, M.O.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.