메뉴 건너뛰기




Volumn 119, Issue 3, 2015, Pages 267-274

Cold-active and NaCl-tolerant exo-inulinase from a cold-adapted Arthrobacter sp. MN8 and its potential for use in the production of fructose at low temperatures

Author keywords

Arthrobacter; Cold active; Exo inulinase; Fructose; NaCl

Indexed keywords

AMINO ACIDS; BACTERIOLOGY; CLONING; ESCHERICHIA COLI; FRUCTOSE; GENES; LEAD COMPOUNDS; POLYSACCHARIDES; PURIFICATION; SODIUM CHLORIDE; ZINC COMPOUNDS;

EID: 84922799557     PISSN: 13891723     EISSN: 13474421     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2014.08.003     Document Type: Article
Times cited : (21)

References (43)
  • 1
    • 0027444372 scopus 로고
    • Evolutionary origins and natural functions of fructans - a climatological, biogeographic and mechanistic appraisal
    • Hendry G.A.F. Evolutionary origins and natural functions of fructans - a climatological, biogeographic and mechanistic appraisal. New Phytol. 1993, 123:3-14.
    • (1993) New Phytol. , vol.123 , pp. 3-14
    • Hendry, G.A.F.1
  • 2
    • 79960854797 scopus 로고    scopus 로고
    • Production and properties of microbial inulinases: recent advances
    • Kango N., Jain S.C. Production and properties of microbial inulinases: recent advances. Food Biotechnol. 2011, 25:165-212.
    • (2011) Food Biotechnol. , vol.25 , pp. 165-212
    • Kango, N.1    Jain, S.C.2
  • 4
    • 33745816040 scopus 로고    scopus 로고
    • Production of inulinases: recent advances
    • Singh P., Gill P.K. Production of inulinases: recent advances. Food Technol. Biotechnol. 2006, 44:151-162.
    • (2006) Food Technol. Biotechnol. , vol.44 , pp. 151-162
    • Singh, P.1    Gill, P.K.2
  • 6
    • 0029074981 scopus 로고
    • Purification and characterization of the Bacillus subtilis levanase produced in Escherichia coli
    • Wanker E., Huber A., Schwab H. Purification and characterization of the Bacillus subtilis levanase produced in Escherichia coli. Appl. Environ. Microbiol. 1995, 61:1953-1958.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1953-1958
    • Wanker, E.1    Huber, A.2    Schwab, H.3
  • 7
    • 2542457331 scopus 로고    scopus 로고
    • Purification and characterization of an exoinulinase from Aspergillus fumigatus
    • Gill P.K., Manhas R.K., Singh J., Singh P. Purification and characterization of an exoinulinase from Aspergillus fumigatus. Appl. Biochem. Biotechnol. 2004, 117:19-32.
    • (2004) Appl. Biochem. Biotechnol. , vol.117 , pp. 19-32
    • Gill, P.K.1    Manhas, R.K.2    Singh, J.3    Singh, P.4
  • 8
    • 50549102307 scopus 로고    scopus 로고
    • Exo-inulinase of Aspergillus niger N402: a hydrolytic enzyme with significant transfructosylating activity
    • Goosen C., Van der Maarel M., Dijkhuizen L. Exo-inulinase of Aspergillus niger N402: a hydrolytic enzyme with significant transfructosylating activity. Biocatal. Biotrans. 2008, 26:49-58.
    • (2008) Biocatal. Biotrans. , vol.26 , pp. 49-58
    • Goosen, C.1    Van der Maarel, M.2    Dijkhuizen, L.3
  • 9
    • 84861127032 scopus 로고    scopus 로고
    • Cloning and sequencing of inulinase and β-fructofuranosidase genes of a deep-sea microbulbifer species and properties of recombinant enzymes
    • Kobayashi T., Uchimura K., Deguchi S., Horikoshi K. Cloning and sequencing of inulinase and β-fructofuranosidase genes of a deep-sea microbulbifer species and properties of recombinant enzymes. Appl. Environ. Microbiol. 2012, 78:2493-2495.
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 2493-2495
    • Kobayashi, T.1    Uchimura, K.2    Deguchi, S.3    Horikoshi, K.4
  • 11
    • 0034130664 scopus 로고    scopus 로고
    • Cloning and characterization of Pseudomonas mucidolens exoinulinase
    • Kwon Y.M., Kim H.Y., Choi Y.J. Cloning and characterization of Pseudomonas mucidolens exoinulinase. J.Microbiol. Biotechnol. 2000, 10:238-243.
    • (2000) J.Microbiol. Biotechnol. , vol.10 , pp. 238-243
    • Kwon, Y.M.1    Kim, H.Y.2    Choi, Y.J.3
  • 12
    • 0031855806 scopus 로고    scopus 로고
    • Analysis of the gene for β-fructosidase (invertase, inulinase) of the hyperthermophilic bacterium Thermotoga maritima, and characterisation of the enzyme expressed in Escherichia coli
    • Liebl W., Brem D., Gotschlich A. Analysis of the gene for β-fructosidase (invertase, inulinase) of the hyperthermophilic bacterium Thermotoga maritima, and characterisation of the enzyme expressed in Escherichia coli. Appl. Microbiol. Biotechnol. 1998, 50:55-64.
    • (1998) Appl. Microbiol. Biotechnol. , vol.50 , pp. 55-64
    • Liebl, W.1    Brem, D.2    Gotschlich, A.3
  • 13
    • 0344784873 scopus 로고    scopus 로고
    • Purification and properties of an extracellular exoinulinase from Penicillium sp. strain TN-88 and sequence analysis of the encoding gene
    • Moriyama S., Akimoto H., Suetsugu N., Kawasaki S., Nakamura T., Ohta K. Purification and properties of an extracellular exoinulinase from Penicillium sp. strain TN-88 and sequence analysis of the encoding gene. Biosci. Biotechnol. Biochem. 2002, 66:1887-1896.
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 1887-1896
    • Moriyama, S.1    Akimoto, H.2    Suetsugu, N.3    Kawasaki, S.4    Nakamura, T.5    Ohta, K.6
  • 14
    • 0345059759 scopus 로고    scopus 로고
    • Molecular cloning and characterization of an exoinulinase gene from Aspergillus niger strain 12 and its expression in Pichia pastoris
    • Moriyama S., Tanaka H., Uwataki M., Muguruma M., Ohta K. Molecular cloning and characterization of an exoinulinase gene from Aspergillus niger strain 12 and its expression in Pichia pastoris. J.Biosci. Bioeng. 2003, 96:324-331.
    • (2003) J.Biosci. Bioeng. , vol.96 , pp. 324-331
    • Moriyama, S.1    Tanaka, H.2    Uwataki, M.3    Muguruma, M.4    Ohta, K.5
  • 15
    • 33750960795 scopus 로고    scopus 로고
    • Purification and characterization of heat-stable exo-inulinase from Streptomyces sp.
    • Sharma A.D., Gill P.K. Purification and characterization of heat-stable exo-inulinase from Streptomyces sp. J.Food Eng. 2007, 79:1172-1178.
    • (2007) J.Food Eng. , vol.79 , pp. 1172-1178
    • Sharma, A.D.1    Gill, P.K.2
  • 17
    • 81255159153 scopus 로고    scopus 로고
    • Cloning of exoinulinase gene from Penicillium janthinellum strain B01 and its high-level expression in Pichia pastoris
    • Wang L., Huang Y., Long X., Meng X., Liu Z. Cloning of exoinulinase gene from Penicillium janthinellum strain B01 and its high-level expression in Pichia pastoris. J.Appl. Microbiol. 2011, 111:1371-1380.
    • (2011) J.Appl. Microbiol. , vol.111 , pp. 1371-1380
    • Wang, L.1    Huang, Y.2    Long, X.3    Meng, X.4    Liu, Z.5
  • 18
    • 13844298153 scopus 로고    scopus 로고
    • Inhibition of glucose on an exoinulinase from Kluyveromyces marxianus expressed in Pichia pastoris
    • Zhang L.H., Zhao C.X., Ohta W.Y., Wang Y.J. Inhibition of glucose on an exoinulinase from Kluyveromyces marxianus expressed in Pichia pastoris. Process Biochem. 2005, 40:1541-1545.
    • (2005) Process Biochem. , vol.40 , pp. 1541-1545
    • Zhang, L.H.1    Zhao, C.X.2    Ohta, W.Y.3    Wang, Y.J.4
  • 21
    • 0035319086 scopus 로고    scopus 로고
    • Potential of halotolerant and halophilic microorganisms for biotechnology
    • Margesin R., Schinner F. Potential of halotolerant and halophilic microorganisms for biotechnology. Extremophiles 2001, 5:73-83.
    • (2001) Extremophiles , vol.5 , pp. 73-83
    • Margesin, R.1    Schinner, F.2
  • 22
    • 70349685126 scopus 로고    scopus 로고
    • Gene cloning, expression and characterization of a new cold-active and salt-tolerant endo-β-1,4-xylanase from marine Glaciecola mesophila KMM 241
    • Guo B., Chen X.L., Sun C.Y., Zhou B.C., Zhang Y.Z. Gene cloning, expression and characterization of a new cold-active and salt-tolerant endo-β-1,4-xylanase from marine Glaciecola mesophila KMM 241. Appl. Microbiol. Biotechnol. 2009, 84:1107-1115.
    • (2009) Appl. Microbiol. Biotechnol. , vol.84 , pp. 1107-1115
    • Guo, B.1    Chen, X.L.2    Sun, C.Y.3    Zhou, B.C.4    Zhang, Y.Z.5
  • 23
    • 79955631894 scopus 로고    scopus 로고
    • Characterization of a novel GH10 thermostable, halophilic xylanase from the marine bacterium Thermoanaerobacterium saccharolyticum NTOU1
    • Hung K.S., Liu S.M., Tzou W.S., Lin F.P., Pan C.L., Fang T.Y., Sun K.H., Tang S.J. Characterization of a novel GH10 thermostable, halophilic xylanase from the marine bacterium Thermoanaerobacterium saccharolyticum NTOU1. Process Biochem. 2011, 46:1257-1263.
    • (2011) Process Biochem. , vol.46 , pp. 1257-1263
    • Hung, K.S.1    Liu, S.M.2    Tzou, W.S.3    Lin, F.P.4    Pan, C.L.5    Fang, T.Y.6    Sun, K.H.7    Tang, S.J.8
  • 24
    • 82755197035 scopus 로고    scopus 로고
    • Purification and some properties of low-molecular-weight extreme halophilic xylanase from Chromohalobacter sp. TPSV 101
    • Prakash B., Vidyasagar M., Jayalakshmi S.K., Sreeramulu K. Purification and some properties of low-molecular-weight extreme halophilic xylanase from Chromohalobacter sp. TPSV 101. J.Mol. Catal. B-Enzym. 2012, 74:192-198.
    • (2012) J.Mol. Catal. B-Enzym. , vol.74 , pp. 192-198
    • Prakash, B.1    Vidyasagar, M.2    Jayalakshmi, S.K.3    Sreeramulu, K.4
  • 25
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0
    • Tamura K., Dudley J., Nei M., Kumar S. MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol. Biol. Evol. 2007, 24:1596-1599.
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 26
    • 77949301366 scopus 로고    scopus 로고
    • Cloning of a new xylanase gene from Streptomyces sp. TN119 using a modified thermal asymmetric interlaced-PCR specific for GC-rich genes and biochemical characterization
    • Zhou J.P., Huang H.Q., Meng K., Shi P.J., Wang Y.R., Luo H.Y., Yang P.L., Bai Y.G., Yao B. Cloning of a new xylanase gene from Streptomyces sp. TN119 using a modified thermal asymmetric interlaced-PCR specific for GC-rich genes and biochemical characterization. Appl. Biochem. Biotechnol. 2010, 160:1277-1292.
    • (2010) Appl. Biochem. Biotechnol. , vol.160 , pp. 1277-1292
    • Zhou, J.P.1    Huang, H.Q.2    Meng, K.3    Shi, P.J.4    Wang, Y.R.5    Luo, H.Y.6    Yang, P.L.7    Bai, Y.G.8    Yao, B.9
  • 27
    • 0017184389 scopus 로고
    • Arapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. Arapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 28
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver H., Burk D. The determination of enzyme dissociation constants. J.Am. Chem. Soc. 1934, 56:658-666.
    • (1934) J.Am. Chem. Soc. , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 29
    • 2442495179 scopus 로고    scopus 로고
    • Cloning, expression, and purification of exoinulinase from Bacillus sp. snu-7
    • Kim K.Y., Koo B.S., Jo D., Kim S.I. Cloning, expression, and purification of exoinulinase from Bacillus sp. snu-7. J.Microbiol. Biotechnol. 2004, 14:344-349.
    • (2004) J.Microbiol. Biotechnol. , vol.14 , pp. 344-349
    • Kim, K.Y.1    Koo, B.S.2    Jo, D.3    Kim, S.I.4
  • 31
    • 0037426296 scopus 로고    scopus 로고
    • Characterization of cold-active dehydrogenases for secondary alcohols and glycerol in psychrotolerant bacteria isolated from Antarctic soil
    • Stibor M., Potocky M., Pickova A., Karasova P., Russell N.J., Kralova B. Characterization of cold-active dehydrogenases for secondary alcohols and glycerol in psychrotolerant bacteria isolated from Antarctic soil. Enzyme Microb. Technol. 2003, 32:532-538.
    • (2003) Enzyme Microb. Technol. , vol.32 , pp. 532-538
    • Stibor, M.1    Potocky, M.2    Pickova, A.3    Karasova, P.4    Russell, N.J.5    Kralova, B.6
  • 32
    • 79953286439 scopus 로고    scopus 로고
    • Molecular characterization of cold-inducible β-galactosidase from Arthrobacter sp. ON14 isolated from Antarctica
    • Xu K., Tang X.A., Gai Y.B., Mehmood M.A., Xiao X.A., Wang F.P. Molecular characterization of cold-inducible β-galactosidase from Arthrobacter sp. ON14 isolated from Antarctica. J.Microbiol. Biotechnol. 2011, 21:236-242.
    • (2011) J.Microbiol. Biotechnol. , vol.21 , pp. 236-242
    • Xu, K.1    Tang, X.A.2    Gai, Y.B.3    Mehmood, M.A.4    Xiao, X.A.5    Wang, F.P.6
  • 33
    • 0035816221 scopus 로고    scopus 로고
    • Modular structure, local flexibility and cold-activity of a novel chitobiase from a psychrophilic Antarctic bacterium
    • Lonhienne T., Zoidakis J., Vorgias C.E., Feller G., Gerday C., Bouriotis V. Modular structure, local flexibility and cold-activity of a novel chitobiase from a psychrophilic Antarctic bacterium. J.Mol. Biol. 2001, 310:291-297.
    • (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
  • 34
    • 80054959848 scopus 로고    scopus 로고
    • Overexpression of the endo-inulinase gene from Arthrobacter sp. S37 in Yarrowia lipolytica and characterization of the recombinant endo-inulinase
    • Li Y., Liu G.L., Wang K., Chi Z.M., Madzak C. Overexpression of the endo-inulinase gene from Arthrobacter sp. S37 in Yarrowia lipolytica and characterization of the recombinant endo-inulinase. J.Mol. Catal. B-Enzym. 2012, 74:109-115.
    • (2012) J.Mol. Catal. B-Enzym. , vol.74 , pp. 109-115
    • Li, Y.1    Liu, G.L.2    Wang, K.3    Chi, Z.M.4    Madzak, C.5
  • 35
    • 78650821698 scopus 로고    scopus 로고
    • Anovel cold-active xylanase gene from the environmental DNA of goat rumen contents: direct cloning, expression and enzyme characterization
    • Wang G., Luo H., Wang Y., Huang H., Shi P., Yang P., Meng K., Bai Y., Yao B. Anovel cold-active xylanase gene from the environmental DNA of goat rumen contents: direct cloning, expression and enzyme characterization. Bioresour. Technol. 2011, 102:3330-3336.
    • (2011) Bioresour. Technol. , vol.102 , pp. 3330-3336
    • Wang, G.1    Luo, H.2    Wang, Y.3    Huang, H.4    Shi, P.5    Yang, P.6    Meng, K.7    Bai, Y.8    Yao, B.9
  • 36
    • 77950340101 scopus 로고    scopus 로고
    • Axylanase with broad pH and temperature adaptability from Streptomyces megasporus DSM 41476, and its potential application in brewing industry
    • Qiu Z., Shi P., Luo H., Bai Y., Yuan T., Yang P., Liu S., Yao B. Axylanase with broad pH and temperature adaptability from Streptomyces megasporus DSM 41476, and its potential application in brewing industry. Enzyme Microb. Technol. 2010, 46:506-512.
    • (2010) Enzyme Microb. Technol. , vol.46 , pp. 506-512
    • Qiu, Z.1    Shi, P.2    Luo, H.3    Bai, Y.4    Yuan, T.5    Yang, P.6    Liu, S.7    Yao, B.8
  • 37
    • 84869875109 scopus 로고    scopus 로고
    • Molecular characterization of a cold-active recombinant xylanase from Flavobacterium johnsoniae and its applicability in xylan hydrolysis
    • Chen S., Kaufman M.G., Miazgowicz K.L., Bagdasarian M., Walker E.D. Molecular characterization of a cold-active recombinant xylanase from Flavobacterium johnsoniae and its applicability in xylan hydrolysis. Bioresour. Technol. 2013, 128:145-155.
    • (2013) Bioresour. Technol. , vol.128 , pp. 145-155
    • Chen, S.1    Kaufman, M.G.2    Miazgowicz, K.L.3    Bagdasarian, M.4    Walker, E.D.5
  • 39
    • 82455209074 scopus 로고    scopus 로고
    • Anovel low-temperature-active β-glucosidase from symbiotic Serratia sp. TN49 reveals four essential positions for substrate accommodation
    • Zhou J.P., Zhang R., Shi P.J., Huang H.Q., Meng K., Yuan T.Z., Yang P.L., Yao B. Anovel low-temperature-active β-glucosidase from symbiotic Serratia sp. TN49 reveals four essential positions for substrate accommodation. Appl. Microbiol. Biotechnol. 2011, 92:305-315.
    • (2011) Appl. Microbiol. Biotechnol. , vol.92 , pp. 305-315
    • Zhou, J.P.1    Zhang, R.2    Shi, P.J.3    Huang, H.Q.4    Meng, K.5    Yuan, T.Z.6    Yang, P.L.7    Yao, B.8
  • 41
    • 33847690260 scopus 로고    scopus 로고
    • Non-digestible oligosaccharides: a review
    • Mussatto S.I., Mancilha I.M. Non-digestible oligosaccharides: a review. Carbohydr. Polym. 2007, 68:587-597.
    • (2007) Carbohydr. Polym. , vol.68 , pp. 587-597
    • Mussatto, S.I.1    Mancilha, I.M.2
  • 42
    • 84856757011 scopus 로고    scopus 로고
    • Properties of the inulinase gene levH1 of Lactobacillus casei IAM 1045; cloning, mutational and biochemical characterization
    • Kuzuwa S., Yokoi K., Kondo M., Kimoto H., Yamakawa A., Taketo A., Kodaira K.I. Properties of the inulinase gene levH1 of Lactobacillus casei IAM 1045; cloning, mutational and biochemical characterization. Gene 2012, 495:154-162.
    • (2012) Gene , vol.495 , pp. 154-162
    • Kuzuwa, S.1    Yokoi, K.2    Kondo, M.3    Kimoto, H.4    Yamakawa, A.5    Taketo, A.6    Kodaira, K.I.7
  • 43
    • 31344453821 scopus 로고    scopus 로고
    • Purification and properties of a heat-stable exoinulinase isoform from Aspergillus fumigatus
    • Gill P.K., Manhas R.K., Singh P. Purification and properties of a heat-stable exoinulinase isoform from Aspergillus fumigatus. Bioresour. Technol. 2006, 97:894-902.
    • (2006) Bioresour. Technol. , vol.97 , pp. 894-902
    • Gill, P.K.1    Manhas, R.K.2    Singh, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.