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Volumn 25, Issue 9, 2009, Pages 1633-1642

Gene cloning, expression and characterization of an α-galactosidase from Pedobacter nyackensis MJ11 CGMCC 2503 with potential as an aquatic feed additive

Author keywords

Galactosidase; Cloning; Expression; Pedobacter nyackensis

Indexed keywords

AMINO ACID SEQUENCE; FEED ADDITIVES; FRESHWATER FISHES; GALACTOSIDASES; GENE CLONING; GLYCOSIDE HYDROLASES; OPTIMAL ACTIVITY; OPTIMUM TEMPERATURE; STACHYOSE; SUBSTRATE SPECIFICITY;

EID: 71349087575     PISSN: 09593993     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11274-009-0057-8     Document Type: Article
Times cited : (4)

References (44)
  • 1
    • 0035807420 scopus 로고    scopus 로고
    • Multiple α-galactosidases from Aspergillus niger: Purification, characterization and substrate specificities
    • doi:10.1016/S0141-0229(01)00415-X
    • Ademark P, Larsson M, Tjerneld F, Stalbrand H (2001) Multiple α-galactosidases from Aspergillus niger: purification, characterization and substrate specificities. Enzyme Microb Technol 29: 441-448. doi: 10. 1016/S0141-0229(01)00415-X.
    • (2001) Enzyme Microb Technol , vol.29 , pp. 441-448
    • Ademark, P.1    Larsson, M.2    Tjerneld, F.3    Stalbrand, H.4
  • 2
    • 0344776744 scopus 로고
    • The use of soy products and other plant protein supplements in aquaculture feeds
    • Akiyama DM (1991) The use of soy products and other plant protein supplements in aquaculture feeds. ASA Tech Bull 27: 1-18.
    • (1991) ASA Tech Bull , vol.27 , pp. 1-18
    • Akiyama, D.M.1
  • 3
    • 0034646605 scopus 로고    scopus 로고
    • Structural, kinetic, and calorimetric characterization of the cold-active phosphoglycerate kinase from the antarctic Pseudomonas sp. TACII18
    • doi:10.1074/jbc.275.15.11147
    • Bentahir M, Feller G, Aittaleb M, Lamotte-Brasseur J, Himri T, Chessa JP, Gerday C (2000) Structural, kinetic, and calorimetric characterization of the cold-active phosphoglycerate kinase from the antarctic Pseudomonas sp. TACII18. J Biol Chem 275: 11147-11153. doi: 10. 1074/jbc. 275. 15. 11147.
    • (2000) J Biol Chem , vol.275 , pp. 11147-11153
    • Bentahir, M.1    Feller, G.2    Aittaleb, M.3    Lamotte-brasseur, J.4    Himri, T.5    Chessa, J.P.6    Gerday, C.7
  • 4
    • 0006275388 scopus 로고
    • Human α-galctosidase A: Nucleotide sequence of a cDNA clone encoding the mature enzyme
    • doi:10.1073/pnas.83.13.4859
    • Bishop DF, Calhoun DH, Berntein HS, Hantzopoulos P, Quinn M, Desnick RJ (1986) Human α-galctosidase A: Nucleotide sequence of a cDNA clone encoding the mature enzyme. Proc Natl Acad Sci USA 83: 4859-4863. doi: 10. 1073/pnas. 83. 13. 4859.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 4859-4863
    • Bishop, D.F.1    Calhoun, D.H.2    Berntein, H.S.3    Hantzopoulos, P.4    Quinn, M.5    Desnick, R.J.6
  • 5
    • 33645240785 scopus 로고    scopus 로고
    • Identification of a novel α-galactosidase from the hyperthermophilic archaeon sulfolobus solfataricus
    • doi:10.1128/JB.188.7.2392-2399.2006
    • Brouns SJJ, Smits N, Wu H, Snijders APL, Wright PC, de Vos WM, van der Oost J (2006) Identification of a novel α-galactosidase from the hyperthermophilic archaeon sulfolobus solfataricus. J Bacteriol 188: 2392-2399. doi: 10. 1128/JB. 188. 7. 2392-2399. 2006.
    • (2006) J Bacteriol , vol.188 , pp. 2392-2399
    • Brouns, S.J.J.1    Smits, N.2    Wu, H.3    Snijders, A.P.L.4    Wright, P.C.5    de Vos, W.M.6    van der Oost, J.7
  • 6
    • 34548456824 scopus 로고    scopus 로고
    • Purification and characterization of a novel protease-resistant α-galactosidase from Rhizopus sp. F78 ACCC 30795
    • doi:10.1016/j.enzmictec.2007.07.005
    • Cao Y, Yang P, Shi P, Wang Y, Luo H, Meng K, Zhang Z, Wu N, Yao B, Fan Y (2007) Purification and characterization of a novel protease-resistant α-galactosidase from Rhizopus sp. F78 ACCC 30795. Enzyme Microb Technol 41: 835-841. doi: 10. 1016/j. enzmictec. 2007. 07. 005.
    • (2007) Enzyme Microb Technol , vol.41 , pp. 835-841
    • Cao, Y.1    Yang, P.2    Shi, P.3    Wang, Y.4    Luo, H.5    Meng, K.6    Zhang, Z.7    Wu, N.8    Yao, B.9    Fan, Y.10
  • 7
    • 50649083965 scopus 로고    scopus 로고
    • Cloning and functional expression of an alpha-galactosidase from Yersinia pestis biovar Microtus str 91001
    • doi:10.1271/bbb.80145
    • Cao Y, Huang H, Meng K, Yang P, Shi P, Wang Y, Luo H, Zhang Z, Wu N, Yao B (2008) Cloning and functional expression of an alpha-galactosidase from Yersinia pestis biovar Microtus str 91001. Biosci Biotechnol Biochem 72: 2203-2205. doi: 10. 1271/bbb. 80145.
    • (2008) Biosci Biotechnol Biochem , vol.72 , pp. 2203-2205
    • Cao, Y.1    Huang, H.2    Meng, K.3    Yang, P.4    Shi, P.5    Wang, Y.6    Luo, H.7    Zhang, Z.8    Wu, N.9    Yao, B.10
  • 8
    • 33845877173 scopus 로고    scopus 로고
    • An α-galactosidase with an essential function during leaf development
    • doi:10.1007/s00425-006-0350-9
    • Chrost B, Kolukisaoglu U, Schulz B, Krupinska K (2007) An α-galactosidase with an essential function during leaf development. Planta 225: 311-320. doi: 10. 1007/s00425-006-0350-9.
    • (2007) Planta , vol.225 , pp. 311-320
    • Chrost, B.1    Kolukisaoglu, U.2    Schulz, B.3    Krupinska, K.4
  • 9
    • 0033949347 scopus 로고    scopus 로고
    • A comparison of enzyme-aided bleaching of softwood paper pulp using combinations of xylanase, mannanase and α-galactosidase
    • doi:10.1007/s002530000344
    • Clarke JH, Davidson K, Rixon JE, Halstead JR, Fransen MP, Gilbert HJ, Hazlewood GP (2000) A comparison of enzyme-aided bleaching of softwood paper pulp using combinations of xylanase, mannanase and α-galactosidase. Appl Microbiol Biotechnol 53: 661-667. doi: 10. 1007/s002530000344.
    • (2000) Appl Microbiol Biotechnol , vol.53 , pp. 661-667
    • Clarke, J.H.1    Davidson, K.2    Rixon, J.E.3    Halstead, J.R.4    Fransen, M.P.5    Gilbert, H.J.6    Hazlewood, G.P.7
  • 10
    • 0035514013 scopus 로고    scopus 로고
    • Characterization of two new glycosyl hydrolases from lactic acid bacterium Carnobacterium piscicola strain BA
    • doi:10.1128/AEM.67.11.5094-5099.2001
    • Coombs J, Brenchley JE (2001) Characterization of two new glycosyl hydrolases from lactic acid bacterium Carnobacterium piscicola strain BA. Appl Environ Microbiol 67: 5094-5099. doi: 10. 1128/AEM. 67. 11. 5094-5099. 2001.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 5094-5099
    • Coombs, J.1    Brenchley, J.E.2
  • 13
    • 84982024062 scopus 로고
    • Induction of alpha-galactosidase in Penicillium ochrochloron by guar (Cyamopsis tetragonobola) gum
    • Dey PM, Patel S, Brownleader MD (1993) Induction of alpha-galactosidase in Penicillium ochrochloron by guar (Cyamopsis tetragonobola) gum. Biotechnol Appl Biochem 17: 361-371.
    • (1993) Biotechnol Appl Biochem , vol.17 , pp. 361-371
    • Dey, P.M.1    Patel, S.2    Brownleader, M.D.3
  • 15
    • 0032876272 scopus 로고    scopus 로고
    • Cloning of the gene encoding a novel thermostable α-galactosidase from thermus brockianus ITI360
    • Fridjonsson O, Watzlawick H, Gehweiler A, Rohrhirsch T, Mattes R (1999) Cloning of the gene encoding a novel thermostable α-galactosidase from thermus brockianus ITI360. Appl Environ Microbiol 65: 3955-3963.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 3955-3963
    • Fridjonsson, O.1    Watzlawick, H.2    Gehweiler, A.3    Rohrhirsch, T.4    Mattes, R.5
  • 16
    • 0344246932 scopus 로고    scopus 로고
    • A novel alkaline α-galactosidase from melon fruit with a substrate preference for raffinose
    • doi:10.1104/pp.119.3.979
    • Gao Z, Schaffer AA (1999) A novel alkaline α-galactosidase from melon fruit with a substrate preference for raffinose. Plant Physiol 119: 979-987. doi: 10. 1104/pp. 119. 3. 979.
    • (1999) Plant Physiol , vol.119 , pp. 979-987
    • Gao, Z.1    Schaffer, A.A.2
  • 17
    • 0029669440 scopus 로고    scopus 로고
    • Purification of α-galactosidase from Lactobacillus fermentum
    • doi:10.1016/0168-1656(95)00149-2
    • Garro MS, de Valdez GF, Oliver G, de Giori GS (1996) Purification of α-galactosidase from Lactobacillus fermentum. J Biotechnol 45: 103-109. doi: 10. 1016/0168-1656(95)00149-2.
    • (1996) J Biotechnol , vol.45 , pp. 103-109
    • Garro, M.S.1    de Valdez, G.F.2    Oliver, G.3    de Giori, G.S.4
  • 19
    • 67349257141 scopus 로고    scopus 로고
    • A novel beta-propeller phytase from Pedobacter nyackensis MJ11 CGMCC 2503 with potential as an aquatic feed additive
    • Huang H, Shao N, Wang Y, Luo H, Yang P, Zhou Z, Zhan Z, Yao B (2009) A novel beta-propeller phytase from Pedobacter nyackensis MJ11 CGMCC 2503 with potential as an aquatic feed additive. Appl Microbiol Biotechnol 83: 249-259. doi: 10. 1007/s00253-008-1835-1.
    • (2009) Appl Microbiol Biotechnol , vol.83 , pp. 249-259
    • Huang, H.1    Shao, N.2    Wang, Y.3    Luo, H.4    Yang, P.5    Zhou, Z.6    Zhan, Z.7    Yao, B.8
  • 20
    • 33644523744 scopus 로고    scopus 로고
    • A food-grade expression/secretion vector for Lactococcus lactis that uses an α-galactosidase gene as a selection marker
    • doi:10.1016/j.fm.2005.06.003
    • Jeonga DW, Leeb JH, Kimc KH, Leea HJ (2006) A food-grade expression/secretion vector for Lactococcus lactis that uses an α-galactosidase gene as a selection marker. Food Microbiol 23: 468-475. doi: 10. 1016/j. fm. 2005. 06. 003.
    • (2006) Food Microbiol , vol.23 , pp. 468-475
    • Jeonga, D.W.1    Leeb, J.H.2    Kimc, K.H.3    Leea, H.J.4
  • 21
    • 33745616255 scopus 로고    scopus 로고
    • Cold-Adapted Enzymes
    • doi:10.1146/annurev.biochem.75.103004.142723
    • Khawar SS, Ricardo C (2006) Cold-Adapted Enzymes. Annu Rev Biochem 75: 403-433. doi: 10. 1146/annurev. biochem. 75. 103004. 142723.
    • (2006) Annu Rev Biochem , vol.75 , pp. 403-433
    • Khawar, S.S.1    Ricardo, C.2
  • 22
    • 20944441182 scopus 로고    scopus 로고
    • Cloning and expression of the gene encoding Streptomyces coelicolor A3(2) alpha-galactosidase belonging to family 36
    • doi:10.1007/s10529-005-3660-2
    • Kondoh K, Morisaki K, Kim W, Park G, Kaneko S, Kobayashi H (2005) Cloning and expression of the gene encoding Streptomyces coelicolor A3(2) alpha-galactosidase belonging to family 36. Biotechnol Lett 27: 641-647. doi: 10. 1007/s10529-005-3660-2.
    • (2005) Biotechnol Lett , vol.27 , pp. 641-647
    • Kondoh, K.1    Morisaki, K.2    Kim, W.3    Park, G.4    Kaneko, S.5    Kobayashi, H.6
  • 23
    • 16644392563 scopus 로고    scopus 로고
    • Reduction of non-digestible oligosaccharides in soymilk: Application of engineered lactic acid bacteria that produce α-galactosidase
    • LeBlanc JG, Silvestroni A, Connes C, Juillard V, de Giori GS, Piard JC (2004) Reduction of non-digestible oligosaccharides in soymilk: application of engineered lactic acid bacteria that produce α-galactosidase. Genet Mol Res 3: 432-440.
    • (2004) Genet Mol Res , vol.3 , pp. 432-440
    • Leblanc, J.G.1    Silvestroni, A.2    Connes, C.3    Juillard, V.4    de Giori, G.S.5    Piard, J.C.6
  • 24
    • 0344549848 scopus 로고    scopus 로고
    • Residue determinants and sequence analysis of cold-adapted trypsins
    • doi:10.1007/s007920050118
    • Leiros HK, Willassen NP, Smalas AO (1999) Residue determinants and sequence analysis of cold-adapted trypsins. Extremophiles 3: 205-219. doi: 10. 1007/s007920050118.
    • (1999) Extremophiles , vol.3 , pp. 205-219
    • Leiros, H.K.1    Willassen, N.P.2    Smalas, A.O.3
  • 25
    • 33847239497 scopus 로고    scopus 로고
    • Expression of Rice (Oryza sativa L. var. Nipponbare) α-galactosidase genes in Escherichia coli and characterization
    • doi:10.1271/bbb.60554
    • Li S, Kim WD, Kaneko S, Prema PA, Nakajima M, Kobayashi H (2007) Expression of Rice (Oryza sativa L. var. Nipponbare) α-galactosidase genes in Escherichia coli and characterization. Biosci Biotechnol Biochem 71: 520-526. doi: 10. 1271/bbb. 60554.
    • (2007) Biosci Biotechnol Biochem , vol.71 , pp. 520-526
    • Li, S.1    Kim, W.D.2    Kaneko, S.3    Prema, P.A.4    Nakajima, M.5    Kobayashi, H.6
  • 26
    • 0020126902 scopus 로고
    • Immobilized α-D-galactosidase in the sugar beet industry
    • doi:10.1016/0141-0229(82)90103-X
    • Linden JC (1982) Immobilized α-D-galactosidase in the sugar beet industry. Enzyme Microb Technol 4: 130-136. doi: 10. 1016/0141-0229(82)90103-X.
    • (1982) Enzyme Microb Technol , vol.4 , pp. 130-136
    • Linden, J.C.1
  • 27
    • 0035816221 scopus 로고    scopus 로고
    • Modular structure, local flexibility and cold-activity of a novel chitobiase from a psychrophilic antarctic bacterium
    • doi:10.1006/jmbi.2001.4774
    • Lonhienne T, Zoidakis J, Vorgias CE, Feller G, Gerday C, Bouriotis V (2001) Modular structure, local flexibility and cold-activity of a novel chitobiase from a psychrophilic antarctic bacterium. J Mol Biol 310: 291-297. doi: 10. 1006/jmbi. 2001. 4774.
    • (2001) J Mol Biol , vol.310 , pp. 291-297
    • Lonhienne, T.1    Zoidakis, J.2    Vorgias, C.E.3    Feller, G.4    Gerday, C.5    Bouriotis, V.6
  • 28
    • 57549112195 scopus 로고    scopus 로고
    • Antarctic, cold-adapted-galactosidase of Pseudoalteromonas sp. 22b as an effective tool for alkyl galactopyranosides synthesis
    • doi:10.1016/j.enzmictec.2008.09.010
    • Makowski K, Białkowska A, Olczak J, Kur J, Turkiewicz M (2009) Antarctic, cold-adapted-galactosidase of Pseudoalteromonas sp. 22b as an effective tool for alkyl galactopyranosides synthesis. Enzyme Microb Technol 44: 59-64. doi: 10. 1016/j. enzmictec. 2008. 09. 010.
    • (2009) Enzyme Microb Technol , vol.44 , pp. 59-64
    • Makowski, K.1    Białkowska, A.2    Olczak, J.3    Kur, J.4    Turkiewicz, M.5
  • 29
    • 33847675844 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel α-galactosidase gene from Penicillium sp. F63 CGMCC 1669 and expression in Pichia pastoris
    • doi:10.1016/j.enzmictec.2006.10.017
    • Mi S, Meng K, Wang Y, Bai Y, Yuan T, Luo H, Yao B (2007) Molecular cloning and characterization of a novel α-galactosidase gene from Penicillium sp. F63 CGMCC 1669 and expression in Pichia pastoris. Enzyme Microb Technol 40: 1373-1380. doi: 10. 1016/j. enzmictec. 2006. 10. 017.
    • (2007) Enzyme Microb Technol , vol.40 , pp. 1373-1380
    • Mi, S.1    Meng, K.2    Wang, Y.3    Bai, Y.4    Yuan, T.5    Luo, H.6    Yao, B.7
  • 30
    • 0029553390 scopus 로고
    • Enzymic hydrolysis of raffinose and stachyose in soymilk by alpha-galactosidase from Gibberella fujikuroi
    • Mulimani VH, Ramalingam (1995) Enzymic hydrolysis of raffinose and stachyose in soymilk by alpha-galactosidase from Gibberella fujikuroi. Biochem Mol Biol Int 36: 897-905.
    • (1995) Biochem Mol Biol Int , vol.36 , pp. 897-905
    • Mulimani, V.H.1    Ramalingam2
  • 31
    • 0032521220 scopus 로고    scopus 로고
    • Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium
    • doi:10.1016/S0969-2126(98)00037-9
    • Russell RJ, Gerike U, Danson MJ, Hough DW, Taylor GL (1998) Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium. Structure 6: 351-361. doi: 10. 1016/S0969-2126(98)00037-9.
    • (1998) Structure , vol.6 , pp. 351-361
    • Russell, R.J.1    Gerike, U.2    Danson, M.J.3    Hough, D.W.4    Taylor, G.L.5
  • 35
    • 0036841521 scopus 로고    scopus 로고
    • Characterization of the melA locus for α-galactosidase in Lactobacillus plantarum
    • doi:10.1128/AEM.68.11.5464-5471.2002
    • Silvestroni A, Connes C, Sesma F, De Giori SG, Piard JC (2002) Characterization of the melA locus for α-galactosidase in Lactobacillus plantarum. Appl Environ Microbiol 68: 5464-5471. doi: 10. 1128/AEM. 68. 11. 5464-5471. 2002.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 5464-5471
    • Silvestroni, A.1    Connes, C.2    Sesma, F.3    de Giori, S.G.4    Piard, J.C.5
  • 36
    • 0034731469 scopus 로고    scopus 로고
    • Approaches for deciphering the structural basis of low temperature enzyme activity
    • doi:10.1016/S0167-4838(00)00237-5
    • Sheridan PP, Panasik N, Coombs JM, Brenchley JE (2000) Approaches for deciphering the structural basis of low temperature enzyme activity. Biochim Biophys Acta 1543: 417-433. doi: 10. 1016/S0167-4838(00)00237-5.
    • (2000) Biochim Biophys Acta , vol.1543 , pp. 417-433
    • Sheridan, P.P.1    Panasik, N.2    Coombs, J.M.3    Brenchley, J.E.4
  • 38
    • 30344486952 scopus 로고    scopus 로고
    • Characterisation of an α-galactosidase with potential relevance to ripening related texture changes
    • doi:10.1016/j.phytochem.2005.09.032
    • Soh C, Ali ZM, Lazan H (2006) Characterisation of an α-galactosidase with potential relevance to ripening related texture changes. Phytochemistry 67: 242-254. doi: 10. 1016/j. phytochem. 2005. 09. 032.
    • (2006) Phytochemistry , vol.67 , pp. 242-254
    • Soh, C.1    Ali, Z.M.2    Lazan, H.3
  • 39
    • 0000045271 scopus 로고
    • Effect of soaking, cooking and crude α-galactosidase treatment on the oligosaccharide content of red gram flour
    • doi:10.1002/jsfa.2740610308
    • Somiari RI, Balogh E (1993) Effect of soaking, cooking and crude α-galactosidase treatment on the oligosaccharide content of red gram flour. Sci Food Agric 61: 339-343. doi: 10. 1002/jsfa. 2740610308.
    • (1993) Sci Food Agric , vol.61 , pp. 339-343
    • Somiari, R.I.1    Balogh, E.2
  • 40
    • 3142735349 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of the gene encoding the Clostridium stercorarium α-galactosidase Aga36A in Escherichia coli
    • doi:10.1271/bbb.67.2160
    • Suryani, Kimura T, Sakka K, Ohmiya K (2003) Cloning, sequencing, and expression of the gene encoding the Clostridium stercorarium α-galactosidase Aga36A in Escherichia coli. Biosci Biotechnol Biochem 67: 2160-2166. doi: 10. 1271/bbb. 67. 2160.
    • (2003) Biosci Biotechnol Biochem , vol.67 , pp. 2160-2166
    • Suryani1    Kimura, T.2    Sakka, K.3    Ohmiya, K.4
  • 41
    • 0031762555 scopus 로고    scopus 로고
    • Archaeal cold-adapted proteins: Structural and evolutionary analysis of the elongation factor 2 proteins from psychrophilic, mesophilic and thermophilic methanogens
    • doi:10.1016/S0014-5793(98)01375-1
    • Thomas T, Cavicchioli R (1998) Archaeal cold-adapted proteins: structural and evolutionary analysis of the elongation factor 2 proteins from psychrophilic, mesophilic and thermophilic methanogens. FEBS Lett 439: 281-286. doi: 10. 1016/S0014-5793(98)01375-1.
    • (1998) FEBS Lett , vol.439 , pp. 281-286
    • Thomas, T.1    Cavicchioli, R.2
  • 42
    • 0014478342 scopus 로고
    • Determination of blood glucose using an oxidase peroxidase system with a non-carcinogenic chromogen
    • doi:10.1136/jcp.22.2.158
    • Tinder P (1969) Determination of blood glucose using an oxidase peroxidase system with a non-carcinogenic chromogen. J Clin Pathol 22: 158-161. doi: 10. 1136/jcp. 22. 2. 158.
    • (1969) J Clin Pathol , vol.22 , pp. 158-161
    • Tinder, P.1
  • 43
    • 34547900302 scopus 로고    scopus 로고
    • Enzyme replacement therapy in patients with Fabry's disease
    • Tsuboi K (2007) Enzyme replacement therapy in patients with Fabry's disease. J Int Med Res 35: 574-581.
    • (2007) J Int Med Res , vol.35 , pp. 574-581
    • Tsuboi, K.1


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