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55 DAFTAR PUSTAKA Aghajari, N., Feller, G., Gerday, C., Haser, C. (1998), Crystal structures of the psychrophilic α-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor, Protein Science. 7, 564-572. Cha, W., Yu, E. K. (1993), Purification and Characterization of Bacillus licheniformis α-amilase from Genetically Cloned E. coli NM522, Bull. Korean Chem. Soc. 14 (3), 398-403. Chandrasekaran, M. (1997), Industrial enzymes from marine microorganisms: The Indian scenario, Journal of Marine Biotechnology. 5, 86-89. Chang, T. M., Chuang, Y. C., Su, J. H., Chang, M. C. (1997), Cloning and Sequence Analysis of a Novel Hemolysin Gene (vllY) from Vibrio vulnificus, Applied And Environmental Microbiology. 63 (10), 3851- 3857. Chaplin, Martin. (2007), Water Stucture and Science. Starch. London South Bank University. Dickmanns, A., Ballschmiter, M., Liebl, W., Ficner, R. (2006), Structure of the novel α-amylase AmyC from Thermotoga mritima, Acta Crystallographica. D62, 262-270. Dong, G., Vieille, C., Savchenko, A., Zeikus, J. G. (1997), Cloning, Sequencing, and Expression of the Gene Encoding Extracellular α-amylase from Pyrococcus furiosus and Biochemical Characterization of the Recombinant Enzyme, Applied And Environmental Microbiology. 63 (9), 3569-3576. Farmer III, J. J. (2006), The Family Vibrionaceae, Prokaryotes. 6, 495-507. Goyal, N., Gupta,J. K., Soni, S. K. (2005), A novel raw starch digesting thermostable α-amylase from Bacillus sp. I-3 and it use in the direct hydrolysis of raw potato starch, Enzyme and Microbial Technology. 37, 723-734. Gupta, R., Gigras, P., Mohapatra, H., Goswami, V. K., Chauhan, B. (2003), Microbial α-amylases: a biotechnological perspective, Process Biochemistry. 38, 1599-1616.

Transcript of ISOLASI GEN PENGKODE -AMILASE DARI BAKTERI...

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DAFTAR PUSTAKA

Aghajari, N., Feller, G., Gerday, C., Haser, C. (1998), Crystal structures of the psychrophilic α-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor, Protein Science. 7, 564-572.

Cha, W., Yu, E. K. (1993), Purification and Characterization of Bacillus

licheniformis α-amilase from Genetically Cloned E. coli NM522, Bull. Korean Chem. Soc. 14 (3), 398-403.

Chandrasekaran, M. (1997), Industrial enzymes from marine microorganisms: The

Indian scenario, Journal of Marine Biotechnology. 5, 86-89. Chang, T. M., Chuang, Y. C., Su, J. H., Chang, M. C. (1997), Cloning and

Sequence Analysis of a Novel Hemolysin Gene (vllY) from Vibrio vulnificus, Applied And Environmental Microbiology. 63 (10), 3851-3857.

Chaplin, Martin. (2007), Water Stucture and Science. Starch. London South Bank

University. Dickmanns, A., Ballschmiter, M., Liebl, W., Ficner, R. (2006), Structure of the

novel α-amylase AmyC from Thermotoga mritima, Acta Crystallographica. D62, 262-270.

Dong, G., Vieille, C., Savchenko, A., Zeikus, J. G. (1997), Cloning, Sequencing,

and Expression of the Gene Encoding Extracellular α-amylase from Pyrococcus furiosus and Biochemical Characterization of the Recombinant Enzyme, Applied And Environmental Microbiology. 63 (9), 3569-3576.

Farmer III, J. J. (2006), The Family Vibrionaceae, Prokaryotes. 6, 495-507. Goyal, N., Gupta,J. K., Soni, S. K. (2005), A novel raw starch digesting

thermostable α-amylase from Bacillus sp. I-3 and it use in the direct hydrolysis of raw potato starch, Enzyme and Microbial Technology. 37, 723-734.

Gupta, R., Gigras, P., Mohapatra, H., Goswami, V. K., Chauhan, B. (2003),

Microbial α-amylases: a biotechnological perspective, Process Biochemistry. 38, 1599-1616.

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Jeang, C., Chen, L., Chen, M., Shiau, R. (2002), Cloning of a Gene Encoding Raw-Starch-Digesting Amylase from a Cytophaga sp. and Its Expression in Escherichia coli, Applied And Environmental Microbiology. 68 (7), 3651-3654.

Jorgensen, S., Vorgias, C. E., Antranikian, G. (1997), Cloning, Sequencing,

Characterization, and Expression of an Extracellular α-Amylase from the Hyperthermophilic Archaeon Pyrococcus furiosus in Escherichia coli and Bacillus subtilis, The Journal of Biologycal Chemistry. 278 (11), 9875-9884.

Kelman, D., Kashman, Y., Rosenberg, E., Kushmaro, A., Yossi, L. (2006),

Antimicrobial activity of Red Sea corals, Marine Biology. 149, 357-363. Linden, A., Mayans, O., Meyer-Klaucke, W., Antranikian, G., Wilmanns, M.

(2003), Differential regulation of a hyperthermophilic α-amylase with a novel (Ca, Zn) Two-metal center by zinc, The Journal of Biological Chemistry. 278 (11), 9875-9884.

MacGregor, E., Janeček, Š., Svenson, B. (2001), Relationship of sequence and

structure to specificity in the α-amylase family of enzymes, Biochimica et Biophysica Acta. 1546, 1-20.

National Center for Biotechnology Information (NCBI). (1998), Nucleotide-

nucleotide BLAST. http://www.ncbi.nlm.nih.gov/blast.cgi. Tanggal akses Januari 2008.

National Center for Biotechnology Information (NCBI). (1998), Conserved

Domain Search. http://www.ncbi.nlm.nih.gov/structure/cdd/cddsrv. Tanggal akses Mei 2008.

Najafi, M. F., Kembhavi, A. (2005), One step purification and characterization of

an extracellular α-amilase from marine Vibrio sp., Enzyme and Microbial Technology. 36, 535-539.

Nielsen, J. E., Borchert, T. V. (2001), Protein engineering of bacterial α-amylase,

Biochim. Biophys. Acta. 1543, 253-274. Reddy, N. S., Nimmagadda, A., Rao, K. R. S. S. (2003), An overview of the

microbial α-amylase family, African Journal of Biotechnology. 2 (12), 645-648.

Rudiger, A., Jorgensen, P. L., Antranikian, G. (1995), Isolation and

Characterisation of a Heat-Stable Pullulanase from the Hyperthermophilic Archaeon Pyrococcus woesei after Cloning and Expressionof its Gene in Escherichia coli, Appl. Environ Microbiol. 61, 567-575.

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Sivaramakrishnan, S., Gangadharan, D., Nampoothiri, K. M., Soccol, C. R., Pandey, A. (2006), α-Amylases from Microbial Sources – An Overview on Recent Developments, Food Technol. Biotechnol. 44 (2), 173-184.

Swanson, C. L., Shogren, R. L., Fanta, G. F., Imam, S. H. (1993), Starch-Plastic

Materials-Preparation, Physical Properties, and Biodegradability (A Review of Recent USDA Research), Journal of Environmental Polymer Degradation. 1 (2), 155-166.

Tsunawa, S., Izu, M., Miyagi, M., Kato, I. (1997), Methionin Aminopeptidase

from the Hyperthermophilic Archaeon Pyrococcus furiosus: Molecular Cloning and Overexpression in Escherichia coli of the Gene, and Characteristics of the Enzyme, Journal of Biochemistry. 122, 843-850.

van der Maarel, M. J. E. C., van der Veen, B., Uitdehaag, J. C. M., Leemhuis, H.,

Dijkhuizen, L. (2002), Properties and applications of starch-converting enzymes of the α-amylase family, Journal of Biotechnology. 94, 137-155.

Zhang, W., Sun, L. (2007), Cloning, Characterization, and Molecular Application

of a Beta-Agarase Gene from Vibrio sp. Strain V134∇, Applied Environmental Microbiology. 73 (9), 2825-2831.

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LAMPIRAN

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LAMPIRAN A

Elektroforegram hasil sekuensing Gen 16S rRNA bakteri laut galur lokal

SFNB3

A. Gen 16S rRNA bakteri laut galur lokal SFNB3 dengan primer Bact-F1

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B. Gen 16S rRNA bakteri laut galur lokal SFNB3 dengan primer UniB1

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LAMPIRAN B

Elektroforegram hasil sekuensing fragmen DNA sisipan pada

plasmid rekombinan (Vsp.7)

A. Fragmen DNA sisipan Vsp.7 dengan primer M13F-pUC

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B. Fragmen DNA sisipan Vsp.7 dengan primer M13R-pUC

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LAMPIRAN C

Analisis urutan asam amino pengkode α-amilase pada genus Vibrio dengan

program Conserved Domains dari NCBI

A. Domain yang terdapat pada α-amilase V. parahaemolyticus RIMD

B. Domain pada α-amilase Vibrio sp. Ex25

C. Domain pada α-amilase Vibrio harveyi HY01

D. Domain pada α-amilase Vibrio alginolyticus 12G01

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E. Domain pada α-amilase Vibrio splendidus 12B01

F. Domain pada α-amilase Vibrio cholerae MZO-3

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LAMPIRAN D

Analisis urutan asam amino pengkode α-amilase pada beberapa spesies

dengan program Conserved Domains dari NCBI

A. Domain pada α-amilase Arabidopsis thaliana

B. Domain pada α-amilase B. subtilis

C. Domain pada α-amilase pendegradasi pati mentah Streptomyces vezuelae