메뉴 건너뛰기




Volumn 247, Issue , 2018, Pages 940-946

Enhanced D-tagatose production by spore surface-displayed L-arabinose isomerase from isolated Lactobacillus brevis PC16 and biotransformation

Author keywords

D tagatose; Immobilization; L arabinose isomerase; Lactobacillus brevis; Spore surface display

Indexed keywords

BACTERIOLOGY; RADIOACTIVE WASTE VITRIFICATION;

EID: 85031024795     PISSN: 09608524     EISSN: 18732976     Source Type: Journal    
DOI: 10.1016/j.biortech.2017.09.187     Document Type: Article
Times cited : (58)

References (36)
  • 1
    • 84947765566 scopus 로고    scopus 로고
    • Display of Thermotoga maritima MSB8 nitrilase on the spore surface of Bacillus subtilis using out coat protein CotG as the fusion partner
    • Chen, H., Chen, Z., Ni, Z., Tian, R., Zhang, T., Jia, J., Chen, K., Yang, S., Display of Thermotoga maritima MSB8 nitrilase on the spore surface of Bacillus subtilis using out coat protein CotG as the fusion partner. J. Mol. Catal. B-Enzym. 123 (2016), 73–80.
    • (2016) J. Mol. Catal. B-Enzym. , vol.123 , pp. 73-80
    • Chen, H.1    Chen, Z.2    Ni, Z.3    Tian, R.4    Zhang, T.5    Jia, J.6    Chen, K.7    Yang, S.8
  • 2
    • 85010904852 scopus 로고    scopus 로고
    • Influences of various peptide linkers on the Thermotoga maritima MSB8 nitrilase displayed on the spore surface of Bacillus subtilis
    • Chen, H., Chen, Z., Wu, B., Ullah, J., Zhang, T., Jia, J., Wang, H., Tan, T., Influences of various peptide linkers on the Thermotoga maritima MSB8 nitrilase displayed on the spore surface of Bacillus subtilis. J. Mol. Catal. B-Enzym. 27 (2017), 64–71.
    • (2017) J. Mol. Catal. B-Enzym. , vol.27 , pp. 64-71
    • Chen, H.1    Chen, Z.2    Wu, B.3    Ullah, J.4    Zhang, T.5    Jia, J.6    Wang, H.7    Tan, T.8
  • 3
    • 84937971839 scopus 로고    scopus 로고
    • Surface display of the thermophilic lipase Tm1350 on the spore of Bacillus subtilis by the CotB anchor protein
    • Chen, H., Tian, R., Ni, Z., Zhang, Q., Zhang, T., Chen, Z., Chen, K., Yang, S., Surface display of the thermophilic lipase Tm1350 on the spore of Bacillus subtilis by the CotB anchor protein. Extremophiles 19 (2015), 799–808.
    • (2015) Extremophiles , vol.19 , pp. 799-808
    • Chen, H.1    Tian, R.2    Ni, Z.3    Zhang, Q.4    Zhang, T.5    Chen, Z.6    Chen, K.7    Yang, S.8
  • 4
    • 85001578768 scopus 로고    scopus 로고
    • Effect of linker length and flexibility on the Clostridium thermocellum esterase displayed on Bacillus subtilis spores
    • Chen, H., Wu, B., Zhang, T., Jia, J., Lu, J., Chen, Z., Ni, Z., Tan, T., Effect of linker length and flexibility on the Clostridium thermocellum esterase displayed on Bacillus subtilis spores. Appl. Biochem. Biotechnol. 182 (2017), 168–180.
    • (2017) Appl. Biochem. Biotechnol. , vol.182 , pp. 168-180
    • Chen, H.1    Wu, B.2    Zhang, T.3    Jia, J.4    Lu, J.5    Chen, Z.6    Ni, Z.7    Tan, T.8
  • 5
    • 84944278915 scopus 로고    scopus 로고
    • Expression and display of a novel thermostable esterase from Clostridium thermocellum on the surface of Bacillus subtilis using the CotB anchor protein
    • Chen, H., Zhang, T., Jia, J., Vastermark, A., Tian, R., Ni, Z., Chen, Z., Chen, K., Yang, S., Expression and display of a novel thermostable esterase from Clostridium thermocellum on the surface of Bacillus subtilis using the CotB anchor protein. J. Ind. Microbiol. Biot. 42 (2015), 1439–1448.
    • (2015) J. Ind. Microbiol. Biot. , vol.42 , pp. 1439-1448
    • Chen, H.1    Zhang, T.2    Jia, J.3    Vastermark, A.4    Tian, R.5    Ni, Z.6    Chen, Z.7    Chen, K.8    Yang, S.9
  • 6
    • 84960474733 scopus 로고    scopus 로고
    • Structure of the thermophilic L-arabinose isomerase from Geobacillus kaustophilus reveals metal-mediated intersubunit interactions for activity and thermostability
    • Choi, J.M., Lee, Y.J., Cao, T.P., Shin, S.M., Park, M.K., Lee, H.S., di Luccio, E., Kim, S.B., Lee, S.J., Lee, S.J., Lee, S.H., Lee, D.W., Structure of the thermophilic L-arabinose isomerase from Geobacillus kaustophilus reveals metal-mediated intersubunit interactions for activity and thermostability. Arch. Biochem. Biophys. 596 (2016), 51–62.
    • (2016) Arch. Biochem. Biophys. , vol.596 , pp. 51-62
    • Choi, J.M.1    Lee, Y.J.2    Cao, T.P.3    Shin, S.M.4    Park, M.K.5    Lee, H.S.6    di Luccio, E.7    Kim, S.B.8    Lee, S.J.9    Lee, S.J.10    Lee, S.H.11    Lee, D.W.12
  • 7
    • 36348972810 scopus 로고    scopus 로고
    • Characterization of an L-arabinose isomerase from the Lactobacillus plantarum NC8 strain showing pronounced stability at acidic pH
    • Chouayekh, H., Bejar, W., Rhimi, M., Jelleli, K., Mseddi, M., Bejar, S., Characterization of an L-arabinose isomerase from the Lactobacillus plantarum NC8 strain showing pronounced stability at acidic pH. FEMS Microbiol. Lett. 277 (2007), 260–267.
    • (2007) FEMS Microbiol. Lett. , vol.277 , pp. 260-267
    • Chouayekh, H.1    Bejar, W.2    Rhimi, M.3    Jelleli, K.4    Mseddi, M.5    Bejar, S.6
  • 8
    • 0346814641 scopus 로고
    • A new spectrophotometric method for the detection and determination of keto sugars and trioses
    • Dische, Z., Borenfreund, E., A new spectrophotometric method for the detection and determination of keto sugars and trioses. J. Biol. Chem. 192 (1951), 583–587.
    • (1951) J. Biol. Chem. , vol.192 , pp. 583-587
    • Dische, Z.1    Borenfreund, E.2
  • 9
    • 84989246565 scopus 로고    scopus 로고
    • Production of D-allulose with D-psicose 3-epimerase expressed and displayed on the surface of Bacillus subtilis spores
    • He, W., Jiang, B., Mu, W., Zhang, T., Production of D-allulose with D-psicose 3-epimerase expressed and displayed on the surface of Bacillus subtilis spores. J. Agric. Food Chem. 64 (2016), 7201–7207.
    • (2016) J. Agric. Food Chem. , vol.64 , pp. 7201-7207
    • He, W.1    Jiang, B.2    Mu, W.3    Zhang, T.4
  • 10
    • 84874365109 scopus 로고    scopus 로고
    • New stable anchor protein and peptide linker suitable for successful spore surface display in B. subtilis
    • Hinc, K., Iwanicki, A., Obuchowski, M., New stable anchor protein and peptide linker suitable for successful spore surface display in B. subtilis. Microb. Cell Fact., 12, 2013, 22.
    • (2013) Microb. Cell Fact. , vol.12 , pp. 22
    • Hinc, K.1    Iwanicki, A.2    Obuchowski, M.3
  • 11
    • 78649900473 scopus 로고    scopus 로고
    • Isolation and screening of lactic acid bacteria from Thai traditional fermented fish (Plasom) and production of Plasom from selected strains
    • Hwanhlem, N., Buradaleng, S., Wattanachant, S., Benjakul, S., Tani, A., Maneerat, S., Isolation and screening of lactic acid bacteria from Thai traditional fermented fish (Plasom) and production of Plasom from selected strains. Food Control. 22 (2011), 401–407.
    • (2011) Food Control. , vol.22 , pp. 401-407
    • Hwanhlem, N.1    Buradaleng, S.2    Wattanachant, S.3    Benjakul, S.4    Tani, A.5    Maneerat, S.6
  • 12
    • 85019864324 scopus 로고    scopus 로고
    • Biocatalytic production of D-tagatose: A potential rare sugar with versatile applications
    • Jayamuthunagai, J., Gautam, P., Srisowmeya, G., Chakravarthy, M., Biocatalytic production of D-tagatose: A potential rare sugar with versatile applications. Crit. Rev. Food Sci. Nutr. 57 (2017), 3430–3437.
    • (2017) Crit. Rev. Food Sci. Nutr. , vol.57 , pp. 3430-3437
    • Jayamuthunagai, J.1    Gautam, P.2    Srisowmeya, G.3    Chakravarthy, M.4
  • 13
    • 85016626481 scopus 로고    scopus 로고
    • D-Tagatose production by permeabilized and immobilized Lactobacillus plantarum using whey permeate
    • Jayamuthunagai, J., Srisowmeya, G., Chakravarthy, M., Gautam, P., D-Tagatose production by permeabilized and immobilized Lactobacillus plantarum using whey permeate. Bioresour. Technol. 235 (2017), 250–255.
    • (2017) Bioresour. Technol. , vol.235 , pp. 250-255
    • Jayamuthunagai, J.1    Srisowmeya, G.2    Chakravarthy, M.3    Gautam, P.4
  • 14
    • 34247495517 scopus 로고    scopus 로고
    • Transgalactosylation in a water-solvent biphasic reaction system with beta-galactosidase displayed on the surfaces of Bacillus subtilis spores
    • Kwon, S.J., Jung, H.C., Pan, J.G., Transgalactosylation in a water-solvent biphasic reaction system with beta-galactosidase displayed on the surfaces of Bacillus subtilis spores. Appl. Environ. Microbiol. 73 (2007), 2251–2256.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 2251-2256
    • Kwon, S.J.1    Jung, H.C.2    Pan, J.G.3
  • 15
    • 29144453887 scopus 로고    scopus 로고
    • Characterization of a thermoacidophilic L-arabinose isomerase from Alicyclobacillus acidocaldarius: role of Lys-269 in pH optimum
    • Lee, S.J., Lee, D.W., Choe, E.A., Hong, Y.H., Kim, S.B., Kim, B.C., Pyun, Y.R., Characterization of a thermoacidophilic L-arabinose isomerase from Alicyclobacillus acidocaldarius: role of Lys-269 in pH optimum. Appl. Environ. Microbiol. 71 (2005), 7888–7896.
    • (2005) Appl. Environ. Microbiol. , 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
  • 16
    • 84857916775 scopus 로고    scopus 로고
    • Bioconversion of D-galactose to D-tagatose: continuous packed bed reaction with an immobilized thermostable L-arabinose isomerase and efficient purification by selective microbial degradation
    • Liang, M., Chen, M., Liu, X., Zhai, Y., Liu, X.W., Zhang, H., Xiao, M., Wang, P., Bioconversion of D-galactose to D-tagatose: continuous packed bed reaction with an immobilized thermostable L-arabinose isomerase and efficient purification by selective microbial degradation. Appl. Microbiol. Biotechnol. 93 (2012), 1469–1474.
    • (2012) Appl. Microbiol. Biotechnol. , vol.93 , pp. 1469-1474
    • Liang, M.1    Chen, M.2    Liu, X.3    Zhai, Y.4    Liu, X.W.5    Zhang, H.6    Xiao, M.7    Wang, P.8
  • 17
    • 84904430838 scopus 로고    scopus 로고
    • Efficient production of D-tagatose using a food-grade surface display system
    • Liu, Y., Li, S., Xu, H., Wu, L., Xu, Z., Liu, J., Feng, X., Efficient production of D-tagatose using a food-grade surface display system. J. Agric. Food Chem. 62 (2014), 6756–6762.
    • (2014) J. Agric. Food Chem. , vol.62 , pp. 6756-6762
    • Liu, Y.1    Li, S.2    Xu, H.3    Wu, L.4    Xu, Z.5    Liu, J.6    Feng, X.7
  • 18
    • 84976870686 scopus 로고    scopus 로고
    • Characterization of an L-arabinose isomerase from Bacillus coagulans NL01 and its application for D-tagatose production
    • Mei, W., Wang, L., Zang, Y., Zheng, Z., Ouyang, J., Characterization of an L-arabinose isomerase from Bacillus coagulans NL01 and its application for D-tagatose production. BMC Biotechnol., 16, 2016, 55.
    • (2016) BMC Biotechnol. , vol.16 , pp. 55
    • Mei, W.1    Wang, L.2    Zang, Y.3    Zheng, Z.4    Ouyang, J.5
  • 19
    • 84891624116 scopus 로고    scopus 로고
    • Enzymatic conversion of D-galactose to D-tagatose: cloning, overexpression and characterization of L-arabinose isomerase from Pediococcus pentosaceus PC-5
    • Men, Y., Zhu, Y., Zhang, L., Kang, Z., Izumori, K., Sun, Y., Ma, Y., Enzymatic conversion of D-galactose to D-tagatose: cloning, overexpression and characterization of L-arabinose isomerase from Pediococcus pentosaceus PC-5. Microbiol. Res. 169 (2014), 171–178.
    • (2014) Microbiol. Res. , vol.169 , pp. 171-178
    • Men, Y.1    Zhu, Y.2    Zhang, L.3    Kang, Z.4    Izumori, K.5    Sun, Y.6    Ma, Y.7
  • 20
    • 32944473444 scopus 로고    scopus 로고
    • Increase in D-tagatose production rate by site-directed mutagenesis of L-arabinose isomerase from Geobacillus thermodenitrificans
    • Oh, H.J., Kim, H.J., Oh, D.K., Increase in D-tagatose production rate by site-directed mutagenesis of L-arabinose isomerase from Geobacillus thermodenitrificans. Biotechnol. Lett. 28 (2006), 145–149.
    • (2006) Biotechnol. Lett. , vol.28 , pp. 145-149
    • Oh, H.J.1    Kim, H.J.2    Oh, D.K.3
  • 21
    • 77956598900 scopus 로고    scopus 로고
    • Display of recombinant proteins on Bacillus subtilis spores, using a coat-associated enzyme as the carrier
    • Potot, S., Serra, C.R., Henriques, A.O., Schyns, G., Display of recombinant proteins on Bacillus subtilis spores, using a coat-associated enzyme as the carrier. Appl. Environ. Microbiol. 76 (2010), 5926–5933.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 5926-5933
    • Potot, S.1    Serra, C.R.2    Henriques, A.O.3    Schyns, G.4
  • 22
    • 0024423190 scopus 로고
    • Characterization of a Lactobacillus strain producing white crystals on cheddar cheese
    • Rengpipat, S., Johnson, E.A., Characterization of a Lactobacillus strain producing white crystals on cheddar cheese. Appl. Environ. Microbiol. 55 (1989), 2579–2582.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 2579-2582
    • Rengpipat, S.1    Johnson, E.A.2
  • 23
    • 78650802091 scopus 로고    scopus 로고
    • Production of D-tagatose, a low caloric sweetener during milk fermentation using L-arabinose isomerase
    • Rhimi, M., Chouayekh, H., Gouillouard, I., Maguin, E., Bejar, S., Production of D-tagatose, a low caloric sweetener during milk fermentation using L-arabinose isomerase. Bioresour. Technol. 102 (2011), 3309–3315.
    • (2011) Bioresour. Technol. , vol.102 , pp. 3309-3315
    • Rhimi, M.1    Chouayekh, H.2    Gouillouard, I.3    Maguin, E.4    Bejar, S.5
  • 24
    • 77955665578 scopus 로고    scopus 로고
    • The acid tolerant L-arabinose isomerase from the food grade Lactobacillus sakei 23K is an attractive D-tagatose producer
    • Rhimi, M., Ilhammami, R., Bajic, G., Boudebbouze, S., Maguin, E., Haser, R., Aghajari, N., The acid tolerant L-arabinose isomerase from the food grade Lactobacillus sakei 23K is an attractive D-tagatose producer. Bioresour. Technol. 101 (2010), 9171–9177.
    • (2010) Bioresour. Technol. , vol.101 , pp. 9171-9177
    • Rhimi, M.1    Ilhammami, R.2    Bajic, G.3    Boudebbouze, S.4    Maguin, E.5    Haser, R.6    Aghajari, N.7
  • 25
    • 84866740969 scopus 로고    scopus 로고
    • Bifidobacterium longum L-arabinose isomerase–overexpression in Lactococcus lactis, purification, and characterization
    • Salonen, N., Nyyssola, A., Salonen, K., Turunen, O., Bifidobacterium longum L-arabinose isomerase–overexpression in Lactococcus lactis, purification, and characterization. Appl. Biochem. Biotechnol. 168 (2012), 392–405.
    • (2012) Appl. Biochem. Biotechnol. , vol.168 , pp. 392-405
    • Salonen, N.1    Nyyssola, A.2    Salonen, K.3    Turunen, O.4
  • 26
    • 84880136941 scopus 로고    scopus 로고
    • D-Tagatose production in the presence of borate by resting Lactococcus lactis cells harboring Bifidobacterium longum L-arabinose isomerase
    • Salonen, N., Salonen, K., Leisola, M., Nyyssola, A., D-Tagatose production in the presence of borate by resting Lactococcus lactis cells harboring Bifidobacterium longum L-arabinose isomerase. Bioprocess Biosyst. Eng. 36 (2013), 489–497.
    • (2013) Bioprocess Biosyst. Eng. , vol.36 , pp. 489-497
    • Salonen, N.1    Salonen, K.2    Leisola, M.3    Nyyssola, A.4
  • 27
    • 84894473593 scopus 로고    scopus 로고
    • L-arabinose isomerase and D-xylose isomerase from Lactobacillus reuteri: Characterization, coexpression in the food grade host Lactobacillus plantarum, and application in the conversion of D-galactose and D-glucose
    • Staudigl, P., Haltrich, D., Peterbauer, C.K., L-arabinose isomerase and D-xylose isomerase from Lactobacillus reuteri: Characterization, coexpression in the food grade host Lactobacillus plantarum, and application in the conversion of D-galactose and D-glucose. J. Agric. Food Chem. 62 (2014), 1617–1624.
    • (2014) J. Agric. Food Chem. , vol.62 , pp. 1617-1624
    • Staudigl, P.1    Haltrich, D.2    Peterbauer, C.K.3
  • 28
    • 0033431016 scopus 로고    scopus 로고
    • Classification and identification of strains of Lactobacillus brevis based on electrophoretic characterization of D-lactate dehydrogenase: relationship between D-lactate dehydrogenase and beer-spoilage ability
    • Takahashi, T., Nakakita, Y., Sugiyama, H., Shigyo, T., Shinotsuka, K., Classification and identification of strains of Lactobacillus brevis based on electrophoretic characterization of D-lactate dehydrogenase: relationship between D-lactate dehydrogenase and beer-spoilage ability. J. Biosci. Bioeng. 88 (1999), 500–506.
    • (1999) J. Biosci. Bioeng. , vol.88 , pp. 500-506
    • Takahashi, T.1    Nakakita, Y.2    Sugiyama, H.3    Shigyo, T.4    Shinotsuka, K.5
  • 29
    • 84865272522 scopus 로고    scopus 로고
    • A method for the production of D-tagatose using a recombinant Pichia pastoris strain secreting beta-D-galactosidase from Arthrobacter chlorophenolicus and a recombinant L-arabinose isomerase from Arthrobacter sp. 22c
    • Wanarska, M., Kur, J., A method for the production of D-tagatose using a recombinant Pichia pastoris strain secreting beta-D-galactosidase from Arthrobacter chlorophenolicus and a recombinant L-arabinose isomerase from Arthrobacter sp. 22c. Microb. Cell Fact., 11, 2012, 113.
    • (2012) Microb. Cell Fact. , vol.11 , pp. 113
    • Wanarska, M.1    Kur, J.2
  • 30
    • 85008476037 scopus 로고    scopus 로고
    • Recent progress in Bacillus subtilis spore-surface display: concept, progress, and future
    • Wang, H., Wang, Y., Yang, R., Recent progress in Bacillus subtilis spore-surface display: concept, progress, and future. Appl. Microbiol. Biotechnol. 101 (2017), 933–949.
    • (2017) Appl. Microbiol. Biotechnol. , vol.101 , pp. 933-949
    • Wang, H.1    Wang, Y.2    Yang, R.3
  • 31
    • 79958190243 scopus 로고    scopus 로고
    • Production of N-acetyl-D-neuraminic acid by use of an efficient spore surface display system
    • Xu, X., Gao, C., Zhang, X., Che, B., Ma, C., Qiu, J., Tao, F., Xu, P., Production of N-acetyl-D-neuraminic acid by use of an efficient spore surface display system. Appl. Environ. Microb. 77 (2011), 3197–3201.
    • (2011) Appl. Environ. Microb. , vol.77 , pp. 3197-3201
    • Xu, X.1    Gao, C.2    Zhang, X.3    Che, B.4    Ma, C.5    Qiu, J.6    Tao, F.7    Xu, P.8
  • 32
    • 84925463294 scopus 로고    scopus 로고
    • L-Arabinose isomerase and its use for biotechnological production of rare sugars
    • Xu, Z., Li, S., Feng, X., Liang, J., Xu, H., L-Arabinose isomerase and its use for biotechnological production of rare sugars. Appl. Microbiol. Biotechnol. 98 (2014), 8869–8878.
    • (2014) Appl. Microbiol. Biotechnol. , vol.98 , pp. 8869-8878
    • Xu, Z.1    Li, S.2    Feng, X.3    Liang, J.4    Xu, H.5
  • 33
    • 84858749628 scopus 로고    scopus 로고
    • Production of D-tagatose, a functional sweetener, utilizing alginate immobilized Lactobacillus fermentum CGMCC2921 cells
    • Xu, Z., Li, S., Fu, F., Li, G., Feng, X., Xu, H., Ouyang, P., Production of D-tagatose, a functional sweetener, utilizing alginate immobilized Lactobacillus fermentum CGMCC2921 cells. Appl. Biochem. Biotechnol. 166 (2012), 961–973.
    • (2012) Appl. Biochem. Biotechnol. , vol.166 , pp. 961-973
    • Xu, Z.1    Li, S.2    Fu, F.3    Li, G.4    Feng, X.5    Xu, H.6    Ouyang, P.7
  • 34
    • 79952814999 scopus 로고    scopus 로고
    • A novel L-arabinose isomerase from Lactobacillus fermentum CGMCC2921 for D-tagatose production: gene cloning, purification and characterization
    • Xu, Z., Qing, Y., Li, S., Feng, X., Xu, H., Ouyang, P., A novel L-arabinose isomerase from Lactobacillus fermentum CGMCC2921 for D-tagatose production: gene cloning, purification and characterization. J. Mol. Catal. B-Enzym. 70 (2011), 1–7.
    • (2011) J. Mol. Catal. B-Enzym. , vol.70 , pp. 1-7
    • Xu, Z.1    Qing, Y.2    Li, S.3    Feng, X.4    Xu, H.5    Ouyang, P.6
  • 35
    • 85017172130 scopus 로고    scopus 로고
    • D-Tagatose production by Lactococcus lactis NZ9000 cells harboring Lactobacillus plantarum L-arabinose isomerase
    • Zhang, Y., Fan, Y., Hu, H., Yang, H., Luo, X., Li, Z., Zhou, H., Ma, W., Song, Y., Zhang, T., D-Tagatose production by Lactococcus lactis NZ9000 cells harboring Lactobacillus plantarum L-arabinose isomerase. Indian J. Pharm. Educ. Res. 51 (2017), 288–294.
    • (2017) Indian J. Pharm. Educ. Res. , vol.51 , pp. 288-294
    • Zhang, Y.1    Fan, Y.2    Hu, H.3    Yang, H.4    Luo, X.5    Li, Z.6    Zhou, H.7    Ma, W.8    Song, Y.9    Zhang, T.10
  • 36
    • 79952574164 scopus 로고    scopus 로고
    • Enhanced activity and stability of L-arabinose isomerase by immobilization on aminopropyl glass
    • Zhang, Y.W., Jeya, M., Lee, J.K., Enhanced activity and stability of L-arabinose isomerase by immobilization on aminopropyl glass. Appl. Microbiol. Biotechnol. 89 (2011), 1435–1442.
    • (2011) Appl. Microbiol. Biotechnol. , vol.89 , pp. 1435-1442
    • Zhang, Y.W.1    Jeya, M.2    Lee, J.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.