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Volumn 28, Issue 6, 2011, Pages 814-821

A novel halotolerant xylanase from marine isolate Bacillus subtilis cho40: Gene cloning and sequencing

Author keywords

[No Author keywords available]

Indexed keywords

AGRICULTURAL RESIDUE; BACILLUS SUBTILIS; BIO-ETHANOL PRODUCTION; CARBON SOURCE; EXTRACELLULAR; GENE CLONING; HALOTOLERANT; MARINE BACTERIUM; NONPOLAR AMINO ACIDS; SALT TOLERANT; SERINE RESIDUES; SOLID-STATE FERMENTATION; SUBTILIS; WHEAT BRAN; XYLANASE ACTIVITY; XYLANASE ENZYMES; XYLANASES;

EID: 80052967042     PISSN: 18716784     EISSN: 18764347     Source Type: Journal    
DOI: 10.1016/j.nbt.2011.08.001     Document Type: Article
Times cited : (72)

References (53)
  • 1
    • 12144282020 scopus 로고    scopus 로고
    • Xylanases, xylanase families and extremophilic xylanases
    • Collins T., et al. Xylanases, xylanase families and extremophilic xylanases. FEMS Microbiol. Rev. 2005, 29:3-23.
    • (2005) FEMS Microbiol. Rev. , vol.29 , pp. 3-23
    • Collins, T.1
  • 2
    • 0343036237 scopus 로고    scopus 로고
    • Endo-β-1,4 xylanase families: diverences in catalytic properties
    • Biely P., et al. Endo-β-1,4 xylanase families: diverences in catalytic properties. J. Biotechnol. 1997, 57:151-166.
    • (1997) J. Biotechnol. , vol.57 , pp. 151-166
    • Biely, P.1
  • 3
    • 33748691219 scopus 로고    scopus 로고
    • Application of thermoalkalophilic xylanase from Arthrobacter sp. MTCC 5214 in biobleaching of kraft pulp
    • Khandeparkar R., Bhosle N.B. Application of thermoalkalophilic xylanase from Arthrobacter sp. MTCC 5214 in biobleaching of kraft pulp. Bioresour. Technol. 2007, 98:897-903.
    • (2007) Bioresour. Technol. , vol.98 , pp. 897-903
    • Khandeparkar, R.1    Bhosle, N.B.2
  • 4
    • 0022386956 scopus 로고
    • Microbial xylanolytic systems
    • Biely P. Microbial xylanolytic systems. Trends Biotechnol. 1985, 3:286-290.
    • (1985) Trends Biotechnol. , vol.3 , pp. 286-290
    • Biely, P.1
  • 5
    • 0001294606 scopus 로고
    • The influence of dietary xylanase on intestinal viscosity and molecular weight distribution of carbohydrates in rye-fed broiler chick
    • Elsevier, J. Visser, BeldmanG, M.A.K. vanSomeren, A.G.J. Voragen (Eds.)
    • Bedford M.R., Classen H.L. The influence of dietary xylanase on intestinal viscosity and molecular weight distribution of carbohydrates in rye-fed broiler chick. Xylans and xylanases 1992, 361-370. Elsevier. J. Visser, BeldmanG, M.A.K. vanSomeren, A.G.J. Voragen (Eds.).
    • (1992) Xylans and xylanases , pp. 361-370
    • Bedford, M.R.1    Classen, H.L.2
  • 6
    • 0000491882 scopus 로고
    • Xylanases and their applications in bakery
    • Elsevier, J. Visser, G. Beldman, M.A. Austers-van Someran, A.G.J. Voragen (Eds.)
    • Maat J., et al. Xylanases and their applications in bakery. Xylan and xylanases 1992, 349-360. Elsevier. J. Visser, G. Beldman, M.A. Austers-van Someran, A.G.J. Voragen (Eds.).
    • (1992) Xylan and xylanases , pp. 349-360
    • Maat, J.1
  • 7
    • 0001088039 scopus 로고
    • Trichoderma xylanases, their properties and purification
    • Wong K.K.Y., Saddler J.N. Trichoderma xylanases, their properties and purification. Crit. Rev. Biotechnol. 1992, 12:413-435.
    • (1992) Crit. Rev. Biotechnol. , vol.12 , pp. 413-435
    • Wong, K.K.Y.1    Saddler, J.N.2
  • 8
    • 0027843477 scopus 로고
    • Lignocellulose biotechnology: current and future prospects
    • Kuhad R.C., Singh A. Lignocellulose biotechnology: current and future prospects. Crit. Rev. Biotechnol. 1993, 13:151-172.
    • (1993) Crit. Rev. Biotechnol. , vol.13 , pp. 151-172
    • Kuhad, R.C.1    Singh, A.2
  • 9
    • 0034126851 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression in Escherichia coli of the new gene encoding β-1,3-xylanase from a marine bacterium, Vibrio sp. strain XY-214
    • Araki T., et al. Cloning, sequencing, and expression in Escherichia coli of the new gene encoding β-1,3-xylanase from a marine bacterium, Vibrio sp. strain XY-214. Appl. Environ. Microbiol. 2000, 66:1741-1743.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 1741-1743
    • Araki, T.1
  • 10
    • 17844370575 scopus 로고    scopus 로고
    • Comparative study of cellulase and xylanase activity in freshwater crayfish and marine prawns
    • Crawford A.C., et al. Comparative study of cellulase and xylanase activity in freshwater crayfish and marine prawns. Aquat. Res. 2005, 36:586-592.
    • (2005) Aquat. Res. , vol.36 , pp. 586-592
    • Crawford, A.C.1
  • 11
    • 0029008857 scopus 로고
    • Identification of a novel cellulose-binding domain within the multidomain 120kDa xylanase XynA of the hyperthermophilic bacterium Thermotoga maritima
    • Winterhalter C., et al. Identification of a novel cellulose-binding domain within the multidomain 120kDa xylanase XynA of the hyperthermophilic bacterium Thermotoga maritima. Mol. Microbiol. 1995, 61:1810-1815.
    • (1995) Mol. Microbiol. , vol.61 , pp. 1810-1815
    • Winterhalter, C.1
  • 12
    • 0000143226 scopus 로고
    • Interactive effect of temperature and salinity on growth and activity of a salt marsh isolate of Aurobasidium pullulans
    • Torzilli A.P., et al. Interactive effect of temperature and salinity on growth and activity of a salt marsh isolate of Aurobasidium pullulans. Mycologia 1985, 77:278-284.
    • (1985) Mycologia , vol.77 , pp. 278-284
    • Torzilli, A.P.1
  • 13
    • 21744449952 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel β-1,3-xylanase possessing two putative carbohydrate-binding modules from a marine bacterium Vibrio sp. strain AX-4
    • Kiyohara M., et al. Molecular cloning and characterization of a novel β-1,3-xylanase possessing two putative carbohydrate-binding modules from a marine bacterium Vibrio sp. strain AX-4. Biochem. J. 2005, 388:949-957.
    • (2005) Biochem. J. , vol.388 , pp. 949-957
    • Kiyohara, M.1
  • 14
    • 33646025832 scopus 로고    scopus 로고
    • Purification and characterization of thermoalkalophilic xylanase isolated from the Enterobacter sp. MTCC 5112
    • Khandeparkar R., Bhosle N. Purification and characterization of thermoalkalophilic xylanase isolated from the Enterobacter sp. MTCC 5112. Res. Microbiol. 2006, 157:315-325.
    • (2006) Res. Microbiol. , vol.157 , pp. 315-325
    • Khandeparkar, R.1    Bhosle, N.2
  • 15
    • 33745206322 scopus 로고    scopus 로고
    • Isolation, purification and characterization of the xylanase produced by Arthrobacter sp. MTCC 5214 when grown in solid-state fermentation
    • Khandeparkar R., Bhosle N. Isolation, purification and characterization of the xylanase produced by Arthrobacter sp. MTCC 5214 when grown in solid-state fermentation. Enzyme Microb. Technol. 2006, 39:732-742.
    • (2006) Enzyme Microb. Technol. , vol.39 , pp. 732-742
    • Khandeparkar, R.1    Bhosle, N.2
  • 16
    • 0642368518 scopus 로고    scopus 로고
    • Production of β-xylanase and β xylosidase by the extremely halophilic archaeon Halorhabdus utahensis
    • Waino M., Ingvorsen K. Production of β-xylanase and β xylosidase by the extremely halophilic archaeon Halorhabdus utahensis. Extremophiles 2003, 7:87-93.
    • (2003) Extremophiles , vol.7 , pp. 87-93
    • Waino, M.1    Ingvorsen, K.2
  • 17
    • 3042825524 scopus 로고    scopus 로고
    • Purification and characterization of two extremely halotolerant xylanases from a novel halophilic bacterium
    • Wejse P.L., et al. Purification and characterization of two extremely halotolerant xylanases from a novel halophilic bacterium. Extremophiles 2003, 7:423-431.
    • (2003) Extremophiles , vol.7 , pp. 423-431
    • Wejse, P.L.1
  • 18
    • 0037457709 scopus 로고    scopus 로고
    • B. Xylanase production by a novel halophilic bacterium increased 20-fold by response surface methodology
    • Wejse P.L., et al. b. Xylanase production by a novel halophilic bacterium increased 20-fold by response surface methodology. Enzyme Microb. Technol. 2003, 32:721-727.
    • (2003) Enzyme Microb. Technol. , vol.32 , pp. 721-727
    • Wejse, P.L.1
  • 19
    • 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., et al. 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
  • 20
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugars
    • Miller G.L. Use of dinitrosalicylic acid reagent for determination of reducing sugars. Anal. Chem. 1959, 31:426-428.
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 21
    • 0029070906 scopus 로고
    • Use of Arabidopsis thaliana defense-related mutants to dissect the plant response to pathogens
    • Ausubel F.M., et al. Use of Arabidopsis thaliana defense-related mutants to dissect the plant response to pathogens. Proc. Natl. Acad. Sci. U.S.A. 1995, 92:4189-4196.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 4189-4196
    • Ausubel, F.M.1
  • 22
    • 0026067797 scopus 로고
    • 16S ribosomal DNA amplification for phylogenetic study
    • Weisburg W.G., et al. 16S ribosomal DNA amplification for phylogenetic study. J. Bacteriol. 1991, 173:697-703.
    • (1991) J. Bacteriol. , vol.173 , pp. 697-703
    • Weisburg, W.G.1
  • 23
    • 29944447809 scopus 로고    scopus 로고
    • Cloning, sequencing and expression of the xylanase gene from a Bacillus subtilis strain B10 in Escherichia coli
    • Huang J., et al. Cloning, sequencing and expression of the xylanase gene from a Bacillus subtilis strain B10 in Escherichia coli. Bioresour. Technol. 2006, 97:802-808.
    • (2006) Bioresour. Technol. , vol.97 , pp. 802-808
    • Huang, J.1
  • 24
    • 0022580815 scopus 로고
    • Xylanase gene from Bacillus subtilis: nucleotide sequence and comparison with B. pumilus gene
    • Paice M.G., et al. xylanase gene from Bacillus subtilis: nucleotide sequence and comparison with B. pumilus gene. Arch. Microbiol. 1986, 144:201-206.
    • (1986) Arch. Microbiol. , vol.144 , pp. 201-206
    • Paice, M.G.1
  • 25
    • 0020032328 scopus 로고
    • Use of Congo-red polysaccharide interactions in enumeration and characterization of cellulolytic bacteria from bovine rumen
    • Teather R.M., Wood P.J. Use of Congo-red polysaccharide interactions in enumeration and characterization of cellulolytic bacteria from bovine rumen. Appl. Environ. Microbiol. 1982, 43:777-782.
    • (1982) Appl. Environ. Microbiol. , vol.43 , pp. 777-782
    • Teather, R.M.1    Wood, P.J.2
  • 27
    • 0025804758 scopus 로고
    • Domains in microbial beta-1,4-glycanases: sequence conservation, function, and enzyme families
    • Gilkes N.R., et al. Domains in microbial beta-1,4-glycanases: sequence conservation, function, and enzyme families. Microbiol. Mol. Biol. Rev. 1991, 55:303-315.
    • (1991) Microbiol. Mol. Biol. Rev. , vol.55 , pp. 303-315
    • Gilkes, N.R.1
  • 28
    • 0027246551 scopus 로고
    • Purification and characterization of a thermostable xylanase from Bacillus stearothermophilus T-6
    • Khasin A., et al. Purification and characterization of a thermostable xylanase from Bacillus stearothermophilus T-6. Appl. Environ. Microbiol. 1993, 59:1725-1730.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 1725-1730
    • Khasin, A.1
  • 29
    • 0029635955 scopus 로고
    • Purification and characterization of a thermophilic alkaline xylanase from thermoalkaliphilic Bacillus sp. strain TAR-l
    • Nakamura S., et al. Purification and characterization of a thermophilic alkaline xylanase from thermoalkaliphilic Bacillus sp. strain TAR-l. J. Mol. Catal. B-Enzyme 1995, 1:7-15.
    • (1995) J. Mol. Catal. B-Enzyme , vol.1 , pp. 7-15
    • Nakamura, S.1
  • 30
    • 0028790376 scopus 로고
    • Purification and properties of xylanase A from alkali-tolerant Bacillus sp. strain BP-23
    • BlankBlanco A., et al. Purification and properties of xylanase A from alkali-tolerant Bacillus sp. strain BP-23. Appl. Environ. Microbiol. 1995, 61:4468-4470.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 4468-4470
    • BlankBlanco, A.1
  • 31
    • 0021835729 scopus 로고
    • Expression of a xylanase gene of Bacillus pumilus in Escherichia coli and Bacillus subtilis
    • Panbangred W., et al. Expression of a xylanase gene of Bacillus pumilus in Escherichia coli and Bacillus subtilis. Appl. Microbiol. Biotechnol. 1985, 22:259-264.
    • (1985) Appl. Microbiol. Biotechnol. , vol.22 , pp. 259-264
    • Panbangred, W.1
  • 32
    • 0000212083 scopus 로고
    • Isolation and characterization of a xylanase from Bacillus subtilis
    • Bemier, et al. Isolation and characterization of a xylanase from Bacillus subtilis. Appl. Environ. Microbiol. 1983, 46:511-514.
    • (1983) Appl. Environ. Microbiol. , vol.46 , pp. 511-514
    • Bemier1
  • 33
    • 84981976048 scopus 로고
    • β-1,4-d-Xylan-degrading enzyme systems: biochemistry, molecular biology, and applications
    • Coughlan M.P., Hazlewood G.P. β-1,4-d-Xylan-degrading enzyme systems: biochemistry, molecular biology, and applications. Biotechnol. Appl. Biochem. 1993, 17:259-289.
    • (1993) Biotechnol. Appl. Biochem. , vol.17 , pp. 259-289
    • Coughlan, M.P.1    Hazlewood, G.P.2
  • 34
    • 0031973584 scopus 로고    scopus 로고
    • Purification and characterisation of a thermostable xylanase from Bacillus amyloliquefaciens
    • Breccia J., et al. Purification and characterisation of a thermostable xylanase from Bacillus amyloliquefaciens. Enzyme Microb. Technol. 1998, 22:42-49.
    • (1998) Enzyme Microb. Technol. , vol.22 , pp. 42-49
    • Breccia, J.1
  • 35
    • 0032033354 scopus 로고    scopus 로고
    • Production, partial purification and characterization of xylanase from Trichosporon cutaneum SL409
    • Liu W., et al. Production, partial purification and characterization of xylanase from Trichosporon cutaneum SL409. Process Biochem. 1998, 33:326-331.
    • (1998) Process Biochem. , vol.33 , pp. 326-331
    • Liu, W.1
  • 36
    • 0034185463 scopus 로고    scopus 로고
    • Class-1 polypeptide chain release factors are structurally and functionally similar to supressor t-RNAs and comprise different structural functional families of prokaryotic/mitochondrial and eukaryotic/archaebacterial factors
    • Kisselev L.L., et al. Class-1 polypeptide chain release factors are structurally and functionally similar to supressor t-RNAs and comprise different structural functional families of prokaryotic/mitochondrial and eukaryotic/archaebacterial factors. Mol. Biol. (Moscow) 2000, 34:427-442.
    • (2000) Mol. Biol. (Moscow) , vol.34 , pp. 427-442
    • Kisselev, L.L.1
  • 37
    • 0033219358 scopus 로고    scopus 로고
    • Purification and characterization of b-1,3-xylanase from a marine bacterium, Vibrio sp. XY-214
    • Araki T., et al. Purification and characterization of b-1,3-xylanase from a marine bacterium, Vibrio sp. XY-214. Biosci. Biotechnol. Biochem. 1999, 63:2017-2019.
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 2017-2019
    • Araki, T.1
  • 38
    • 1842418765 scopus 로고    scopus 로고
    • Purificaton and characterization of xylanases from Aspergillus giganteusa
    • Fialho M.B., Carmona E.C. Purificaton and characterization of xylanases from Aspergillus giganteusa. Folia Microbiol. 2004, 49:13-18.
    • (2004) Folia Microbiol. , vol.49 , pp. 13-18
    • Fialho, M.B.1    Carmona, E.C.2
  • 39
    • 0034105727 scopus 로고    scopus 로고
    • Isolation, purification and characterization of xylanase from Staphylococcus sp. SG-13 and its application in biobleaching of kraft pulp
    • Gupta S., et al. Isolation, purification and characterization of xylanase from Staphylococcus sp. SG-13 and its application in biobleaching of kraft pulp. J. Appl. Microbiol. 2000, 88:325-334.
    • (2000) J. Appl. Microbiol. , vol.88 , pp. 325-334
    • Gupta, S.1
  • 40
    • 3242655750 scopus 로고    scopus 로고
    • Purification and characterization of alkaline xylanases from Pseudomonas G6-2
    • Liu R., et al. Purification and characterization of alkaline xylanases from Pseudomonas G6-2. Wei Sheng Wu Xue Bao 1999, 39:132-136.
    • (1999) Wei Sheng Wu Xue Bao , vol.39 , pp. 132-136
    • Liu, R.1
  • 41
    • 0031126325 scopus 로고    scopus 로고
    • Purification and some properties of endo-1,4-β-d-xylanase from a fresh-water mollusc, Pomacea insularus (de Ordigny)
    • Yamaura I., et al. Purification and some properties of endo-1,4-β-d-xylanase from a fresh-water mollusc, Pomacea insularus (de Ordigny). Biosci. Biotechnol. Biochem. 1997, 61:615-620.
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 615-620
    • Yamaura, I.1
  • 42
    • 21244499811 scopus 로고    scopus 로고
    • Tanapongpipat Sutipa and Kirtikara Kanyawim Endo-1,4-xylanase B from Aspergillus cf. niger BCC14405 isolated in Thailand: purification, characterization and gene isolation
    • Krisana A., et al. Tanapongpipat Sutipa and Kirtikara Kanyawim Endo-1,4-xylanase B from Aspergillus cf. niger BCC14405 isolated in Thailand: purification, characterization and gene isolation. J. Biochem. Mol. Biol. 2005, 38:17-23.
    • (2005) J. Biochem. Mol. Biol. , vol.38 , pp. 17-23
    • Krisana, A.1
  • 43
    • 33846845195 scopus 로고    scopus 로고
    • Molecular cloning and heterologous expression of a new xylanase gene from Plectosphaerella cucumerina
    • Zhang G., et al. Molecular cloning and heterologous expression of a new xylanase gene from Plectosphaerella cucumerina. Appl. Microbiol. Biotechnol. 2007, 74:339-346.
    • (2007) Appl. Microbiol. Biotechnol. , vol.74 , pp. 339-346
    • Zhang, G.1
  • 44
    • 0036090445 scopus 로고    scopus 로고
    • Production, purification and properties of xylanase from a newly isolated Fusarium proliferatum
    • Saha B.C. Production, purification and properties of xylanase from a newly isolated Fusarium proliferatum. Process Biochem. 2002, 37:1279-1284.
    • (2002) Process Biochem. , vol.37 , pp. 1279-1284
    • Saha, B.C.1
  • 45
    • 31144467011 scopus 로고    scopus 로고
    • Isolation and properties of Aspergillus niger IBT-90 xylanase for bakery
    • Irena R., et al. Isolation and properties of Aspergillus niger IBT-90 xylanase for bakery. Appl. Microbiol. Biotechnol. 2006, 69:665-671.
    • (2006) Appl. Microbiol. Biotechnol. , vol.69 , pp. 665-671
    • Irena, R.1
  • 46
    • 4644306667 scopus 로고
    • Electrophoretic differences in seed proteins among varieties of soybean. Glycine max (1) Merrill
    • Larsen A.L. Electrophoretic differences in seed proteins among varieties of soybean. Glycine max (1) Merrill. Crop Sci. 1967, 7:311-313.
    • (1967) Crop Sci. , vol.7 , pp. 311-313
    • Larsen, A.L.1
  • 47
    • 0018866939 scopus 로고
    • Spectrophotometric Identification of the pigment associated with light-driven primary sodium translocation in Halobacterium halobium
    • Lanyi J.K., Weber H.J. Spectrophotometric Identification of the pigment associated with light-driven primary sodium translocation in Halobacterium halobium. J. Biol. Chem. 1980, 255:243-250.
    • (1980) J. Biol. Chem. , vol.255 , pp. 243-250
    • Lanyi, J.K.1    Weber, H.J.2
  • 48
    • 61349118641 scopus 로고    scopus 로고
    • Xylanase production using inexpensive agricultural wastes and its partial characterization from a halophilic Chromohalobacter sp. TPSV 101
    • Prakash S., et al. Xylanase production using inexpensive agricultural wastes and its partial characterization from a halophilic Chromohalobacter sp. TPSV 101. World J. Microbiol. Biotechnol. 2009, 25:197-204.
    • (2009) World J. Microbiol. Biotechnol. , vol.25 , pp. 197-204
    • Prakash, S.1
  • 49
    • 79952677403 scopus 로고    scopus 로고
    • Jha B isolation, purification, and characterization of haloalkaline xylanase from a marine Bacillus pumilus strain
    • Menon G., et al. Jha B isolation, purification, and characterization of haloalkaline xylanase from a marine Bacillus pumilus strain. Biotechnol. Bioprocess. Eng. 2010, 5:998-1005.
    • (2010) Biotechnol. Bioprocess. Eng. , vol.5 , pp. 998-1005
    • Menon, G.1
  • 50
    • 14644442998 scopus 로고    scopus 로고
    • Organic Solvent tolerance of halophilic α-amylase from a Haloarchaeon, Haloarcula sp. strain S-1
    • Fukushima T., et al. Organic Solvent tolerance of halophilic α-amylase from a Haloarchaeon, Haloarcula sp. strain S-1. Extremophiles 2005, 9:85-89.
    • (2005) Extremophiles , vol.9 , pp. 85-89
    • Fukushima, T.1
  • 51
    • 29244438994 scopus 로고    scopus 로고
    • Characterization of a highly stable a-amylase from the halophilic archaeon Haloarcula hispanica
    • Hutcheon G.W., et al. Characterization of a highly stable a-amylase from the halophilic archaeon Haloarcula hispanica. Extremophiles 2005, 9:487-492.
    • (2005) Extremophiles , vol.9 , pp. 487-492
    • Hutcheon, G.W.1
  • 52
    • 33751196772 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular haloalkaline protease produced by the moderately halophilic bacterium, Salinivibrio sp. strain AF-2004
    • Karbalaei-Heidari H.R., et al. Purification and characterization of an extracellular haloalkaline protease produced by the moderately halophilic bacterium, Salinivibrio sp. strain AF-2004. Enzyme Microb. Technol. 2007, 40:266-272.
    • (2007) Enzyme Microb. Technol. , vol.40 , pp. 266-272
    • Karbalaei-Heidari, H.R.1
  • 53
    • 72049123466 scopus 로고    scopus 로고
    • A visionary and conceptual macroalgae-based third generation bioethanol (TGB) biorefinery in Sabah, Malaysia as an underlay for renewable and sustainable development
    • Goh C.S., Lee K.T. A visionary and conceptual macroalgae-based third generation bioethanol (TGB) biorefinery in Sabah, Malaysia as an underlay for renewable and sustainable development. Renew. Sust. Energy Rev. 2010, 14:842-848.
    • (2010) Renew. Sust. Energy Rev. , vol.14 , pp. 842-848
    • Goh, C.S.1    Lee, K.T.2


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