참고문헌
- Lee HS, Kim MS, Cho HS, Kim JI, Kim TJ, Choi JH, Park C, Lee HS, Oh BH, Park KH. Cyclomaltodextrinase, neopullulanase, and maltogenic amylase are nearly indistinguishable from each other. J. Biol. Chem. 277: 21891-21897 (2002) https://doi.org/10.1074/jbc.M201623200
- Oh SW, Jang MU, Jeong CK, Yuk JB, Park JM, Park KH, Kim TJ. Development of detection method for cyclomaltodextrinase family genes using degenerate PCR primers. Food Sci. Biotechnol. 15: 967-974 (2006)
- Park KH. Functional and tertiary- and quaternary-structure of cyclodextrin-hydrolyzing enzymes (CDases), a group of multisubstrate specific enzymes belonging to the amylase family. J. Appl. Glycosci. 53: 35-44 (2006) https://doi.org/10.5458/jag.53.35
- Kuriki T, Imanaka T. Nucleotide sequence of the neopullulanase gene from Bacillus stearothermophilus. J. Gen. Microbiol. 135: 1521-1528 (1989) https://doi.org/10.1099/00221287-135-6-1521
- Kim TJ, Shin JH, Oh JH, Kim MJ, Lee SB, Ryu S, Kwon K, Kim JW, Choi EH, Robyt JF, Park KH. Analysis of the gene encoding cyclomaltodextrinase from alkalophilic Bacillus sp. I-5 and characterization of enzymatic properties. Arch. Biochem. Biophys. 353: 221-227 (1998) https://doi.org/10.1006/abbi.1998.0639
- Cha HJ, Yoon HG, Kim YW, Lee HS, Kim JW, Kweon KS, Oh BH, Park KH. Molecular and enzymatic characterization of a maltogenic amylase that hydrolyzes and transglycosylates acarbose. Eur. J. Biochem. 253: 251-262 (1998) https://doi.org/10.1046/j.1432-1327.1998.2530251.x
- Cho HY, Kim YW, Kim TJ, Lee HS, Kim DY, Kim JW, Lee YW, Leed S, Park KH. Molecular characterization of a dimeric intracellular maltogenic amylase of Bacillus subtilis SUH4-2. Biochim. Biophys. Acta 1478: 333-340 (2000) https://doi.org/10.1016/S0167-4838(00)00037-6
- Cheong KA, Kim TJ, Yoon JW, Park CS, Lee TS, Kim YB, Park KH, Kim JW. Catalytic activities of intracellular dimeric neopullulanase on cyclodextrin, acarbose and maltose. Biotechnol. Appl. Biochem. 35: 27-34 (2002) https://doi.org/10.1042/BA20010052
- Kaulpiboon J, Pongsawasdi P. Expression of cyclodextrinase gene from Paenibacillus sp. A11 in Escherichia coli and characterization of the purified cyclodextrinase. J. Biochem. Mol. Biol. 37: 408-415 (2004) https://doi.org/10.5483/BMBRep.2004.37.4.408
- Podkovyrov SM, Zeikus JG. Structure of the gene encoding cyclomaltodextrinase from Clostridium thermohydrosulfuricum 39E and characterization of the enzyme purified from Escherichia coli. J. Bacteriol. 174: 5400-5405 (1992) https://doi.org/10.1128/jb.174.16.5400-5405.1992
-
Tonozuka T, Ohtsuka M, Mogi S, Sakai H, Ohta T, Sakano Y. A neopullulanase-type
$\alpha$ -amylase gene from Thermoactinomyces vulgaris R-47. Biosci. Biotech. Bioch. 57: 395-401 (1993) https://doi.org/10.1271/bbb.57.395 - Feederle R, Pajatsch M, Kremmer E, Bock A. Metabolism of cyclodextrins by Klebsiella oxytoca M5a1: Purification and characterisation of a cytoplasmically located cyclodextrinase. Arch. Microbiol. 165: 206-212 (1996) https://doi.org/10.1007/s002030050317
- Kim TJ, Kim MJ, Kim BC, Kim JC, Cheong TK, Kim JW, Park KH. Modes of action of acarbose hydrolysis and transglycosylation catalyzed by a thermostable maltogenic amylase, the gene for which was cloned from a Thermus strain. Appl. Environ. Microb. 65: 1644-1651 (1999)
- Oh KW, Kim MJ, Kim HY, Kim BY, Baik MY, Auh JH, Park CS. Enzymatic characterization of a maltogenic amylase from Lactobacillus gasseri ATCC 33323 expressed in Escherichia coli. FEMS Microbiol. Lett. 252: 175-181 (2005) https://doi.org/10.1016/j.femsle.2005.08.050
- Kamitori S, Kondo S, Okuyama K, Yokota T, Shimura Y, Tonozuka T, Sakano Y. Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 resolution. J. Mol. Biol. 287: 907-921 (1999) https://doi.org/10.1006/jmbi.1999.2647
- Kim JS, Cha SS, Kim HJ, Kim TJ, Ha NC, Oh ST, Cho HS, Cho MJ, Kim MJ, Lee HS, Kim JW, Choi KY, Park KH, Oh BH. Crystal structure of a maltogenic amylase provides insight into a catalytic versatility. J. Biol. Chem. 274: 26279-26286 (1999) https://doi.org/10.1074/jbc.274.37.26279
- Hondoh H, Kuriki T, Matsuura Y. Three-dimensional structure and substrate binding of Bacillus stearothermophilus neopullulanase. J. Mol. Biol. 326: 177-188 (2003) https://doi.org/10.1016/S0022-2836(02)01402-X
- Kim TJ, Nguyen VD, Lee HS, Kim MJ, Cho HY, Kim YW, Moon TW, Park CS, Kim JW, Oh BH, Lee SB, Svensson B, Park KH. Modulation of the multisubstrate specificity of Thermus maltogenic amylase by truncation of the N-terminal domain and by a saltinduced shift of the monomer/dimer equilibrium. Biochemistry 40: 14182-14190 (2001) https://doi.org/10.1021/bi015531u
- Park KH, Kim MJ, Lee HS, Han NS, Kim D, Robyt JF. Transglycosylation reactions of Bacillus stearothermophilus maltogenic amylase with acarbose and various acceptors. Carbohyd. Res. 313: 235-246 (1998) https://doi.org/10.1016/S0008-6215(98)00276-6
- Bae HK, Lee SB, Park CS, Shim JH, Lee HY, Kim MJ, Baek JS, Roh HJ, Choi JH, Choe EO, Ahn DU, Park KH. Modification of ascorbic acid using transglycosylation activity of Bacillus stearothermophilus maltogenic amylase to enhance its oxidative stability. J. Agr. Food Chem. 50: 3309-3316 (2002) https://doi.org/10.1021/jf011550z
- Li D, Park SH, Shim JH, Lee HS, Tang SY, Park CS, Park KH. In vitro enzymatic modification of puerarin to puerarin glycosides by maltogenic amylase. Carbohyd. Res. 339: 2789-2797 (2004) https://doi.org/10.1016/j.carres.2004.09.017
- Auh JH, Chae HY, Kim YR, Shim KH, Yoo SH, Park KH. Modification of rice starch by selective degradation of amylose using alkalophilic Bacillus cyclomaltodextrinase. J. Agr. Food Chem. 54: 2314-2319 (2006) https://doi.org/10.1021/jf051887r
- Takami H, Nakasone K, Takaki Y, Maeno G, Sasaki R, Masui N, Fuji F, Hirama C, Nakamura Y, Ogasawara N, Kuhara S, Horikoshi K. Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis. Nucleic Acids Res. 28: 4317-4331 (2000) https://doi.org/10.1093/nar/28.21.4317
-
Park JM, Han NS, Kim TJ. Rapid detection and isolation of known and putative
$\alpha$ -L-arabinofuranosidase genes using degenerate PCR primers. J. Microbiol. Biotechn. 17: 481-489 (2007) - Miller GL. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 31: 426-428 (1959) https://doi.org/10.1021/ac60147a030
- Fleming ID, Pegler HF. The determination of glucose in the presence of maltose and isomaltose by a stable, specific enzymic reagent. Analyst 88: 967-968 (1963) https://doi.org/10.1039/an9638800967
- Park KH, Kim TJ, Cheong TK, Kim JW, Oh BH, Svensson B. Structure, specificity, and function of cyclomaltodextrinase, a multispecific enzyme of the alpha-amylase family. Biochim. Biophys. Acta 1478: 165-185 (2000) https://doi.org/10.1016/S0167-4838(00)00041-8
- Kim JW, Kim YH, Lee HS, Yang SJ, Kim YW, Lee MH, Kim JW, Seo NS, Park CS, Park KH. Molecular cloning and biochemical characterization of the first archael maltogenic amylase from the hyperthermophilic archaeon Thermoplasma volcanium GSS1. Biochim. Biophys. Acta 1774: 661-669 (2007) https://doi.org/10.1016/j.bbapap.2007.03.010
- Oh SW, Jang MU, Jeong CK, Kang HJ, Park JM, Kim TJ. Modulation of substrate specificity and transglycosylation activity of Thermus maltogenic amylase by combinatorial saturation mutagenesis. J. Microbiol. Biotechn. 18: 1401-1407 (2008)