메뉴 건너뛰기




Volumn 177, Issue 7, 2015, Pages 1480-1492

Engineering of Alicyclobacillus hesperidum l-Arabinose Isomerase for Improved Catalytic Activity and Reduced pH Optimum Using Random and Site-Directed Mutagenesis

Author keywords

d tagatose; Error prone PCR; l Arabinose isomerase; Random mutagenesis; Site directed mutagenesis

Indexed keywords

BACILLI; CATALYST ACTIVITY; ISOMERIZATION; ISOMERS; MANGANESE; MUTAGENESIS;

EID: 84947488135     PISSN: 02732289     EISSN: 15590291     Source Type: Journal    
DOI: 10.1007/s12010-015-1828-3     Document Type: Article
Times cited : (20)

References (31)
  • 1
    • 84925463294 scopus 로고    scopus 로고
    • l-Arabinose isomerase and its use for biotechnological production of rare sugars
    • COI: 1:CAS:528:DC%2BC2cXhs12nt7vM
    • Xu, Z., Li, S., Feng, X., Liang, J., & Xu, H. (2014). l-Arabinose isomerase and its use for biotechnological production of rare sugars. Applied Microbiology and Biotechnology,98, 8869–8878.
    • (2014) Applied Microbiology and Biotechnology , vol.98 , pp. 8869-8878
    • Xu, Z.1    Li, S.2    Feng, X.3    Liang, J.4    Xu, H.5
  • 2
    • 34547600568 scopus 로고    scopus 로고
    • Tagatose: properties, applications, and biotechnological processes
    • COI: 1:CAS:528:DC%2BD2sXosVSksrk%3D
    • Oh, D. K. (2007). Tagatose: properties, applications, and biotechnological processes. Applied Microbiology and Biotechnology,76, 1–8.
    • (2007) Applied Microbiology and Biotechnology , vol.76 , pp. 1-8
    • Oh, D.K.1
  • 3
    • 4544346270 scopus 로고    scopus 로고
    • Current studies on biological tagatose production using l-arabinose isomerase: a review and future perspective
    • COI: 1:CAS:528:DC%2BD2cXmsVCgurg%3D
    • Kim, P. (2004). Current studies on biological tagatose production using l-arabinose isomerase: a review and future perspective. Applied Microbiology and Biotechnology,65, 243–249.
    • (2004) Applied Microbiology and Biotechnology , vol.65 , pp. 243-249
    • Kim, P.1
  • 4
    • 0033250151 scopus 로고    scopus 로고
    • d-Tagatose—a novel low-calorie bulk sweetener with prebiotic properties
    • COI: 1:CAS:528:DC%2BD3cXisFSms7s%3D
    • Bertelsen, H., Jensen, B. B., & Buemann, B. (1999). d-Tagatose—a novel low-calorie bulk sweetener with prebiotic properties. World Review of Nutrition and Dietetics,85, 98–109.
    • (1999) World Review of Nutrition and Dietetics , vol.85 , pp. 98-109
    • Bertelsen, H.1    Jensen, B.B.2    Buemann, B.3
  • 5
    • 84904374606 scopus 로고    scopus 로고
    • Recent and emerging therapeutic medications in type 2 diabetes mellitus: incretin-based, pramlintide, colesevelam, SGLT2 inhibitors, tagatose, succinobucol
    • Lo, M. C., & Lansang, M. C. (2013). Recent and emerging therapeutic medications in type 2 diabetes mellitus: incretin-based, pramlintide, colesevelam, SGLT2 inhibitors, tagatose, succinobucol. American Journal of Therapeutics,20, 638–653.
    • (2013) American Journal of Therapeutics , vol.20 , pp. 638-653
    • Lo, M.C.1    Lansang, M.C.2
  • 6
    • 84880861260 scopus 로고    scopus 로고
    • Beneficial effect of tagatose consumption on postprandial hyperglycemia in Koreans: a double-blind crossover designed study
    • COI: 1:CAS:528:DC%2BC3sXhtFKgurnI
    • Kwak, J. H., Kim, M. S., Lee, J. H., Yang, Y. J., Lee, K. H., Kim, O. Y., & Lee, J. H. (2013). Beneficial effect of tagatose consumption on postprandial hyperglycemia in Koreans: a double-blind crossover designed study. Food & Function,4, 1223–1228.
    • (2013) Food & Function , vol.4 , pp. 1223-1228
    • Kwak, J.H.1    Kim, M.S.2    Lee, J.H.3    Yang, Y.J.4    Lee, K.H.5    Kim, O.Y.6    Lee, J.H.7
  • 7
    • 58849155498 scopus 로고    scopus 로고
    • Effect of diets containing sucrose vs. d-tagatose in hypercholesterolemic mice
    • COI: 1:CAS:528:DC%2BD1MXhtVWisbg%3D
    • Police, S. B., Harris, J. C., Lodder, R. A., & Cassis, L. A. (2009). Effect of diets containing sucrose vs. d-tagatose in hypercholesterolemic mice. Obesity,17, 269–275.
    • (2009) Obesity , vol.17 , pp. 269-275
    • Police, S.B.1    Harris, J.C.2    Lodder, R.A.3    Cassis, L.A.4
  • 8
    • 78649936082 scopus 로고    scopus 로고
    • Dietary supplementation with d-tagatose in subjects with type 2 diabetes leads to weight loss and raises high-density lipoprotein cholesterol
    • COI: 1:CAS:528:DC%2BC3cXhsFGgsb3O
    • Donner, T. W., Magder, L. S., & Zarbalian, K. (2010). Dietary supplementation with d-tagatose in subjects with type 2 diabetes leads to weight loss and raises high-density lipoprotein cholesterol. Nutrition Research,30, 801–806.
    • (2010) Nutrition Research , vol.30 , pp. 801-806
    • Donner, T.W.1    Magder, L.S.2    Zarbalian, K.3
  • 9
    • 38049186809 scopus 로고    scopus 로고
    • Tagatose, a new antidiabetic and obesity control drug
    • COI: 1:CAS:528:DC%2BD1cXivVOrtrg%3D
    • Lu, Y., Levin, G. V., & Donner, T. W. (2008). Tagatose, a new antidiabetic and obesity control drug. Diabetes Obesity & Metabolism,10, 109–134.
    • (2008) Diabetes Obesity & Metabolism , vol.10 , pp. 109-134
    • Lu, Y.1    Levin, G.V.2    Donner, T.W.3
  • 10
    • 0036997321 scopus 로고    scopus 로고
    • Removal and prevention of dental plaque with d-tagatose
    • COI: 1:CAS:528:DC%2BD38XnsVSksbs%3D
    • Lu, Y., & Levin, G. V. (2002). Removal and prevention of dental plaque with d-tagatose. International Journal of Cosmetic Science,24, 225–234.
    • (2002) International Journal of Cosmetic Science , vol.24 , pp. 225-234
    • Lu, Y.1    Levin, G.V.2
  • 11
    • 2842525944 scopus 로고    scopus 로고
    • Food browning and its prevention: an overview
    • COI: 1:CAS:528:DyaK28Xht1ylsrs%3D
    • Friedman, M. (1996). Food browning and its prevention: an overview. Journal of Agricultural and Food Chemistry,44, 631–653.
    • (1996) Journal of Agricultural and Food Chemistry , vol.44 , pp. 631-653
    • Friedman, M.1
  • 12
    • 33644629689 scopus 로고    scopus 로고
    • Cloning, purification and biochemical characterization of metallic-ions independent and thermoactive l-arabinose isomerase from the Bacillus stearothermophilus US100 strain
    • COI: 1:CAS:528:DC%2BD28XitVarsLw%3D
    • Rhimi, M., & Bejar, S. (2006). Cloning, purification and biochemical characterization of metallic-ions independent and thermoactive l-arabinose isomerase from the Bacillus stearothermophilus US100 strain. Biochimica et Biophysica Acta,1760, 191–199.
    • (2006) Biochimica et Biophysica Acta , vol.1760 , pp. 191-199
    • Rhimi, M.1    Bejar, S.2
  • 13
    • 33745454160 scopus 로고    scopus 로고
    • Characterization of a mutated Geobacillus stearothermophilus l-arabinose isomerase that increases the production rate of d-tagatose
    • COI: 1:CAS:528:DC%2BD28XotFKgtb4%3D
    • Kim, H. J., Kim, J. H., Oh, H. J., & Oh, D. K. (2006). Characterization of a mutated Geobacillus stearothermophilusl-arabinose isomerase that increases the production rate of d-tagatose. Journal of Applied Microbiology,101, 213–221.
    • (2006) Journal of Applied Microbiology , vol.101 , pp. 213-221
    • Kim, H.J.1    Kim, J.H.2    Oh, H.J.3    Oh, D.K.4
  • 14
    • 26444526645 scopus 로고    scopus 로고
    • Purification and characterization of an l-arabinose isomerase from an isolated strain of Geobacillus thermodenitrificans producing d-tagatose
    • COI: 1:CAS:528:DC%2BD2MXhtFSisLrL
    • Kim, H. J., & Oh, D. K. (2005). Purification and characterization of an l-arabinose isomerase from an isolated strain of Geobacillus thermodenitrificans producing d-tagatose. Journal of Biotechnology,120, 162–173.
    • (2005) Journal of Biotechnology , vol.120 , pp. 162-173
    • Kim, H.J.1    Oh, D.K.2
  • 15
    • 3142713057 scopus 로고    scopus 로고
    • Enzymatic conversion of d-galactose to d-tagatose: heterologous expression and characterisation of a thermostable l-arabinose isomerase from Thermoanaerobacter mathranii
    • COI: 1:CAS:528:DC%2BD2cXktlyrsr4%3D
    • Jorgensen, F., Hansen, O. C., & Stougaard, P. (2004). Enzymatic conversion of d-galactose to d-tagatose: heterologous expression and characterisation of a thermostable l-arabinose isomerase from Thermoanaerobacter mathranii.Applied Microbiology and Biotechnology,64, 816–822.
    • (2004) Applied Microbiology and Biotechnology , vol.64 , pp. 816-822
    • Jorgensen, F.1    Hansen, O.C.2    Stougaard, P.3
  • 16
    • 0037129833 scopus 로고    scopus 로고
    • Cloning, expression and characterization of l-arabinose isomerase from Thermotoga neapolitana: bioconversion of d-galactose to d-tagatose using the enzyme
    • COI: 1:CAS:528:DC%2BD38XksF2jsrY%3D
    • Kim, B. C., Lee, Y. H., Lee, H. S., Lee, D. W., Choe, E. A., & Pyun, Y. R. (2002). Cloning, expression and characterization of l-arabinose isomerase from Thermotoga neapolitana: bioconversion of d-galactose to d-tagatose using the enzyme. FEMS Microbiology Letters,212, 121–126.
    • (2002) FEMS Microbiology Letters , vol.212 , pp. 121-126
    • Kim, B.C.1    Lee, Y.H.2    Lee, H.S.3    Lee, D.W.4    Choe, E.A.5    Pyun, Y.R.6
  • 17
    • 1642416740 scopus 로고    scopus 로고
    • Characterization of a thermostable l-arabinose (d-galactose) isomerase from the hyperthermophilic eubacterium Thermotoga maritima
    • COI: 1:CAS:528:DC%2BD2cXisVKjuro%3D
    • Lee, D. W., Jang, H. J., Choe, E. A., Kim, B. C., Lee, S. J., Kim, S. B., Hong, Y., & Pyun, Y. R. (2004). Characterization of a thermostable l-arabinose (d-galactose) isomerase from the hyperthermophilic eubacterium Thermotoga maritima.Applied and Environmental Microbiology,70, 1397–1404.
    • (2004) Applied and Environmental Microbiology , vol.70 , pp. 1397-1404
    • Lee, D.W.1    Jang, H.J.2    Choe, E.A.3    Kim, B.C.4    Lee, S.J.5    Kim, S.B.6    Hong, Y.7    Pyun, Y.R.8
  • 18
    • 29144453887 scopus 로고    scopus 로고
    • Characterization of a thermoacidophilic l-arabinose isomerase from Alicyclobacillus acidocaldarius: role of Lys-269 in pH optimum
    • COI: 1:CAS:528:DC%2BD2MXhtlehtLjO
    • Lee, S. J., Lee, D. W., Choe, E. A., Hong, Y. H., Kim, S. B., Kim, B. C., & Pyun, Y. R. (2005). Characterization of a thermoacidophilic l-arabinose isomerase from Alicyclobacillus acidocaldarius: role of Lys-269 in pH optimum. Applied and Environmental Microbiology,71, 7888–7896.
    • (2005) Applied and Environmental Microbiology , vol.71 , pp. 7888-7896
    • Lee, S.J.1    Lee, D.W.2    Choe, E.A.3    Hong, Y.H.4    Kim, S.B.5    Kim, B.C.6    Pyun, Y.R.7
  • 19
    • 84899980900 scopus 로고    scopus 로고
    • Function of aspartic acid residues in optimum pH control of l-arabinose isomerase from Lactobacillus fermentum
    • COI: 1:CAS:528:DC%2BC3sXhslKntbvI
    • Xu, Z., Li, S., Feng, X. H., Zhan, Y. J., & Xu, H. (2014). Function of aspartic acid residues in optimum pH control of l-arabinose isomerase from Lactobacillus fermentum.Applied Microbiology and Biotechnology,98, 3987–3996.
    • (2014) Applied Microbiology and Biotechnology , vol.98 , pp. 3987-3996
    • Xu, Z.1    Li, S.2    Feng, X.H.3    Zhan, Y.J.4    Xu, H.5
  • 20
    • 84870979267 scopus 로고    scopus 로고
    • Homologous alkalophilic and acidophilic l-arabinose isomerases reveal region-specific contributions to the pH dependence of activity and stability
    • COI: 1:CAS:528:DC%2BC38XhslyjsrrP
    • Lee, S. J., Lee, Y. J., Kim, S. B., Kim, S. K., & Lee, D. W. (2012). Homologous alkalophilic and acidophilic l-arabinose isomerases reveal region-specific contributions to the pH dependence of activity and stability. Applied and Environmental Microbiology,78, 8813–8816.
    • (2012) Applied and Environmental Microbiology , vol.78 , pp. 8813-8816
    • Lee, S.J.1    Lee, Y.J.2    Kim, S.B.3    Kim, S.K.4    Lee, D.W.5
  • 21
    • 0034775246 scopus 로고    scopus 로고
    • Improvement of tagatose conversion rate by genetic evolution of thermostable galactose isomerase
    • COI: 1:CAS:528:DC%2BD3MXotFWqtbw%3D
    • Kim, P., Yoon, S. H., Seo, M. J., Oh, D. K., & Choi, J. H. (2001). Improvement of tagatose conversion rate by genetic evolution of thermostable galactose isomerase. Biotechnology and Applied Biochemistry,34, 99–102.
    • (2001) Biotechnology and Applied Biochemistry , vol.34 , pp. 99-102
    • Kim, P.1    Yoon, S.H.2    Seo, M.J.3    Oh, D.K.4    Choi, J.H.5
  • 22
    • 84920251559 scopus 로고    scopus 로고
    • Characterization of a F280N variant of l-arabinose isomerase from Geobacillus thermodenitrificans identified as a d-galactose isomerase
    • COI: 1:CAS:528:DC%2BC2cXovFKqtr0%3D
    • Kim, B. J., Hong, S. H., Shin, K. C., Jo, Y. S., & Oh, D. K. (2014). Characterization of a F280N variant of l-arabinose isomerase from Geobacillus thermodenitrificans identified as a d-galactose isomerase. Applied Microbiology and Biotechnology,98, 9271–9281.
    • (2014) Applied Microbiology and Biotechnology , vol.98 , pp. 9271-9281
    • Kim, B.J.1    Hong, S.H.2    Shin, K.C.3    Jo, Y.S.4    Oh, D.K.5
  • 23
    • 84895532582 scopus 로고    scopus 로고
    • Biochemical characterization of a thermostable l-arabinose isomerase from a thermoacidophilic bacterium, Alicyclobacillus hesperidum URH17-3–68
    • COI: 1:CAS:528:DC%2BC2cXlvFCitb0%3D
    • Fan, C., Liu, K., Zhang, T., Zhou, L., Xue, D., Jiang, B., & Mu, W. (2014). Biochemical characterization of a thermostable l-arabinose isomerase from a thermoacidophilic bacterium, Alicyclobacillus hesperidum URH17-3–68. Journal of Molecular Catalysis B-Enzymatic,102, 120–126.
    • (2014) Journal of Molecular Catalysis B-Enzymatic , vol.102 , pp. 120-126
    • Fan, C.1    Liu, K.2    Zhang, T.3    Zhou, L.4    Xue, D.5    Jiang, B.6    Mu, W.7
  • 24
    • 77952501933 scopus 로고    scopus 로고
    • Thermostable l-arabinose isomerase from Bacillus stearothermophilus IAM 11001 for d-tagatose production: gene cloning, purification and characterisation
    • COI: 1:CAS:528:DC%2BC3cXmtV2jsLY%3D
    • Cheng, L., Mu, W., & Jiang, B. (2010). Thermostable l-arabinose isomerase from Bacillus stearothermophilus IAM 11001 for d-tagatose production: gene cloning, purification and characterisation. Journal of the Science of Food and Agriculture,90, 1327–1333.
    • (2010) Journal of the Science of Food and Agriculture , vol.90 , pp. 1327-1333
    • Cheng, L.1    Mu, W.2    Jiang, B.3
  • 25
    • 84862810508 scopus 로고    scopus 로고
    • Heterologous expression and characterization of Bacillus coagulans l-arabinose isomerase
    • COI: 1:CAS:528:DC%2BC38XmtFWgtbc%3D
    • Zhou, X., & Wu, J. C. (2012). Heterologous expression and characterization of Bacillus coagulansl-arabinose isomerase. World Journal of Microbiology & Biotechnology,28, 2205–2212.
    • (2012) World Journal of Microbiology & Biotechnology , vol.28 , pp. 2205-2212
    • Zhou, X.1    Wu, J.C.2
  • 26
    • 77950629696 scopus 로고    scopus 로고
    • An l-arabinose isomerase from Acidothermus cellulolytics ATCC 43068: cloning, expression, purification, and characterization
    • COI: 1:CAS:528:DC%2BC3cXjvVehs78%3D
    • Cheng, L., Mu, W., Zhang, T., & Jiang, B. (2010). An l-arabinose isomerase from Acidothermus cellulolytics ATCC 43068: cloning, expression, purification, and characterization. Applied Microbiology and Biotechnology,86, 1089–1097.
    • (2010) Applied Microbiology and Biotechnology , vol.86 , pp. 1089-1097
    • Cheng, L.1    Mu, W.2    Zhang, T.3    Jiang, B.4
  • 27
    • 79955525190 scopus 로고    scopus 로고
    • Identification and characterization of a novel l-arabinose isomerase from Anoxybacillus flavithermus useful in d-tagatose production
    • Li, Y., Zhu, Y., Liu, A., & Sun, Y. (2011). Identification and characterization of a novel l-arabinose isomerase from Anoxybacillus flavithermus useful in d-tagatose production. Extremophiles,15, 441–450.
    • (2011) Extremophiles , vol.15 , pp. 441-450
    • Li, Y.1    Zhu, Y.2    Liu, A.3    Sun, Y.4
  • 28
    • 33745287171 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli l-arabinose isomerase (ECAI), the putative target of biological tagatose production
    • COI: 1:CAS:528:DC%2BD28Xmt1yrs7Y%3D
    • Manjasetty, B. A., & Chance, M. R. (2006). Crystal structure of Escherichia coli l-arabinose isomerase (ECAI), the putative target of biological tagatose production. Journal of Molecular Biology,360, 297–309.
    • (2006) Journal of Molecular Biology , vol.360 , pp. 297-309
    • Manjasetty, B.A.1    Chance, M.R.2
  • 29
    • 64449084435 scopus 로고    scopus 로고
    • Rational design of Bacillus stearothermophilus US100 l-arabinose isomerase: potential applications for d-tagatose production
    • COI: 1:CAS:528:DC%2BD1MXksVCntLc%3D
    • Rhimi, M., Aghajari, N., Juy, M., Chouayekh, H., Maguin, E., Haser, R., & Bejar, S. (2009). Rational design of Bacillus stearothermophilus US100 l-arabinose isomerase: potential applications for d-tagatose production. Biochimie,91, 650–653.
    • (2009) Biochimie , vol.91 , pp. 650-653
    • Rhimi, M.1    Aghajari, N.2    Juy, M.3    Chouayekh, H.4    Maguin, E.5    Haser, R.6    Bejar, S.7
  • 30
    • 33750616739 scopus 로고    scopus 로고
    • Modification of optimal pH in l-arabinose isomerase from Geobacillus stearothermophilus for d-galactose isomerization
    • COI: 1:CAS:528:DC%2BD28Xht1Sgsb7K
    • Oh, D. K., Oh, H. J., Kim, H. J., Cheon, J., & Kim, P. (2006). Modification of optimal pH in l-arabinose isomerase from Geobacillus stearothermophilus for d-galactose isomerization. Journal of Molecular Catalysis B-Enzymatic,43, 108–112.
    • (2006) Journal of Molecular Catalysis B-Enzymatic , vol.43 , pp. 108-112
    • Oh, D.K.1    Oh, H.J.2    Kim, H.J.3    Cheon, J.4    Kim, P.5
  • 31
    • 32944473444 scopus 로고    scopus 로고
    • Increase in d-tagatose production rate by site-directed mutagenesis of l-arabinose isomerase from Geobacillus thermodenitrificans
    • COI: 1:CAS:528:DC%2BD28XhsFCrsrY%3D
    • Oh, H. J., Kim, H. J., & Oh, D. K. (2006). Increase in d-tagatose production rate by site-directed mutagenesis of l-arabinose isomerase from Geobacillus thermodenitrificans.Biotechnology Letters,28, 145–149.
    • (2006) Biotechnology Letters , vol.28 , pp. 145-149
    • Oh, H.J.1    Kim, H.J.2    Oh, D.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.