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Volumn 91, Issue , 2014, Pages 110-119

Bio-ethanol production through simultaneous saccharification and fermentation using an encapsulated reconstituted cell-free enzyme system

Author keywords

Batch processing; Encapsulation; Enzyme technology; Ethanol; Reconstituted cell free system; Yeast

Indexed keywords

BATCH DATA PROCESSING; BIOETHANOL; ENCAPSULATION; ETHANOL; SACCHARIFICATION; SUBSTRATES; YEAST;

EID: 84907340915     PISSN: 1369703X     EISSN: 1873295X     Source Type: Journal    
DOI: 10.1016/j.bej.2014.08.006     Document Type: Article
Times cited : (44)

References (66)
  • 1
    • 43049115291 scopus 로고    scopus 로고
    • Trends in biotechnological production of fuel ethanol from different feedstocks
    • Oscar J.S., Carlos A.C. Trends in biotechnological production of fuel ethanol from different feedstocks. Bioresour. Technol. 2008, 99:5270-5295.
    • (2008) Bioresour. Technol. , vol.99 , pp. 5270-5295
    • Oscar, J.S.1    Carlos, A.C.2
  • 2
    • 84873567051 scopus 로고    scopus 로고
    • Lipase from Penicillium camembertii KCCM 11268: optimization of solid state fermentation and application to biodiesel production
    • Malilas W., Kang S.W., Kim S.B., Yoo H.Y., Chulalaksananukul W., Kim S.W. Lipase from Penicillium camembertii KCCM 11268: optimization of solid state fermentation and application to biodiesel production. Korean J. Chem. Eng. 2013, 30:405-412.
    • (2013) Korean J. Chem. Eng. , vol.30 , pp. 405-412
    • Malilas, W.1    Kang, S.W.2    Kim, S.B.3    Yoo, H.Y.4    Chulalaksananukul, W.5    Kim, S.W.6
  • 3
    • 84865811730 scopus 로고    scopus 로고
    • Evaluation of sediments of the waste from beer fermentation broth for bioethanol production
    • Ha J.H., Gang M.K., Khan T., Park J.K. Evaluation of sediments of the waste from beer fermentation broth for bioethanol production. Korean J. Chem. Eng. 2012, 29:1224-1231.
    • (2012) Korean J. Chem. Eng. , vol.29 , pp. 1224-1231
    • Ha, J.H.1    Gang, M.K.2    Khan, T.3    Park, J.K.4
  • 5
    • 84868025359 scopus 로고    scopus 로고
    • Comparison of hydrolysis abilities onto soluble and commercial raw starches of immobilized and free B. amyloliquefaciens α-amylase
    • Dincbas S., Demirkan E. Comparison of hydrolysis abilities onto soluble and commercial raw starches of immobilized and free B. amyloliquefaciens α-amylase. J. Biol. Environ. Sci. 2010, 4:87-95.
    • (2010) J. Biol. Environ. Sci. , vol.4 , pp. 87-95
    • Dincbas, S.1    Demirkan, E.2
  • 6
    • 0036159062 scopus 로고    scopus 로고
    • Hydrolysis of lignocellulosic material for ethanol production: a review
    • Sun Y., Cheng J. Hydrolysis of lignocellulosic material for ethanol production: a review. Bioresour. Technol. 2002, 83:1-11.
    • (2002) Bioresour. Technol. , vol.83 , pp. 1-11
    • Sun, Y.1    Cheng, J.2
  • 7
    • 44449146433 scopus 로고    scopus 로고
    • Enzyme-based hydrolysis processes for ethanol from lignocellulosic materials: a review
    • Taherzadeh M.J., Karimi K. Enzyme-based hydrolysis processes for ethanol from lignocellulosic materials: a review. Bioresources 2007, 2:707-738.
    • (2007) Bioresources , vol.2 , pp. 707-738
    • Taherzadeh, M.J.1    Karimi, K.2
  • 8
    • 0027587608 scopus 로고
    • Study of the enzymatic hydrolysis of cellulose for production of fuel ethanol by the simultaneous saccharification and fermentation process
    • Philippidis G.P., Smith T.K., Wyman C.E. Study of the enzymatic hydrolysis of cellulose for production of fuel ethanol by the simultaneous saccharification and fermentation process. Biotechnol. Bioeng. 1993, 41:846-853.
    • (1993) Biotechnol. Bioeng. , vol.41 , pp. 846-853
    • Philippidis, G.P.1    Smith, T.K.2    Wyman, C.E.3
  • 9
    • 84869020456 scopus 로고    scopus 로고
    • Prospects of reusable endogenous hydrolyzing enzymes in bioethanol production by simultaneous saccharification and fermentation
    • Khattak W.A., Ul-Islam M., Park J.K. Prospects of reusable endogenous hydrolyzing enzymes in bioethanol production by simultaneous saccharification and fermentation. Korean J. Chem. Eng. 2012, 29:1467-1482.
    • (2012) Korean J. Chem. Eng. , vol.29 , pp. 1467-1482
    • Khattak, W.A.1    Ul-Islam, M.2    Park, J.K.3
  • 10
    • 84883779803 scopus 로고    scopus 로고
    • Enhanced production of bioethanol from waste of beer fermentation broth at high temperature through consecutive batch strategy by simultaneous saccharification and fermentation
    • Khattak W.A., Khan T., Ha J.H., Ul-Islam M., Kang M.K., Park J.K. Enhanced production of bioethanol from waste of beer fermentation broth at high temperature through consecutive batch strategy by simultaneous saccharification and fermentation. Enzyme Microb. Technol. 2013, 53:322-330.
    • (2013) Enzyme Microb. Technol. , vol.53 , pp. 322-330
    • Khattak, W.A.1    Khan, T.2    Ha, J.H.3    Ul-Islam, M.4    Kang, M.K.5    Park, J.K.6
  • 11
    • 84875876106 scopus 로고    scopus 로고
    • In vitro assembly of minicellulosomes with two scaffoldins on the yeast cell surface for cellulose saccharification and bioethanol production
    • Fan L.H., Zhang Z.J., Yu X.Y., Xue Y.X., Wang M.M., Tan T.W. In vitro assembly of minicellulosomes with two scaffoldins on the yeast cell surface for cellulose saccharification and bioethanol production. Proc. Biochem. 2013, 48:430-437.
    • (2013) Proc. Biochem. , vol.48 , pp. 430-437
    • Fan, L.H.1    Zhang, Z.J.2    Yu, X.Y.3    Xue, Y.X.4    Wang, M.M.5    Tan, T.W.6
  • 13
    • 0032213339 scopus 로고    scopus 로고
    • Thermotolerance in Saccharomyces cerevisiae: the Yin and Yang of trehalose
    • Singer M.A., Lindquist S. Thermotolerance in Saccharomyces cerevisiae: the Yin and Yang of trehalose. Trends Biotechnol. 1998, 16:460-468.
    • (1998) Trends Biotechnol. , vol.16 , pp. 460-468
    • Singer, M.A.1    Lindquist, S.2
  • 14
    • 84907316348 scopus 로고    scopus 로고
    • Simultaneous saccharification and fermentation (SSF) of industrial wastes for production of ethanol
    • Kadar Z., Szengyel Z., Reczey K. Simultaneous saccharification and fermentation (SSF) of industrial wastes for production of ethanol. Ind. Crops Prod. 2004, 2:257-273.
    • (2004) Ind. Crops Prod. , vol.2 , pp. 257-273
    • Kadar, Z.1    Szengyel, Z.2    Reczey, K.3
  • 15
    • 0036385526 scopus 로고    scopus 로고
    • A review of the production of ethanol from softwood
    • Galbe M., Zacchi G. A review of the production of ethanol from softwood. Appl. Microbiol. Biot. 2002, 59:618-628.
    • (2002) Appl. Microbiol. Biot. , vol.59 , pp. 618-628
    • Galbe, M.1    Zacchi, G.2
  • 16
    • 20344403066 scopus 로고    scopus 로고
    • Ethanol production from glucose and dilute-acid hydrolyzates by encapsulated S. cerevisiae
    • Talebnia F., Niklasson C., Taherzadeh M.J. Ethanol production from glucose and dilute-acid hydrolyzates by encapsulated S. cerevisiae. Biotechnol. Bioeng. 2005, 90:345-353.
    • (2005) Biotechnol. Bioeng. , vol.90 , pp. 345-353
    • Talebnia, F.1    Niklasson, C.2    Taherzadeh, M.J.3
  • 17
    • 84876687368 scopus 로고    scopus 로고
    • Obtaining strains of Saccharomyces tolerant to high temperatures and ethanol
    • Peres M.F., Sousa S.R., Laluce C. Obtaining strains of Saccharomyces tolerant to high temperatures and ethanol. Food Microbiol. Protoc. 2000, 14:355-367.
    • (2000) Food Microbiol. Protoc. , vol.14 , pp. 355-367
    • Peres, M.F.1    Sousa, S.R.2    Laluce, C.3
  • 18
    • 84872402351 scopus 로고    scopus 로고
    • Next-generation bioproduction systems: cell-free conversion concepts for industrial biotechnology
    • Rupp S. Next-generation bioproduction systems: cell-free conversion concepts for industrial biotechnology. Eng. Life Sci. 2013, 1:19-25.
    • (2013) Eng. Life Sci. , vol.1 , pp. 19-25
    • Rupp, S.1
  • 19
    • 0035313673 scopus 로고    scopus 로고
    • Industrial biocatalysis
    • Zaks A. Industrial biocatalysis. Curr. Opin. Chem. Biol. 2001, 5:130-136.
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 130-136
    • Zaks, A.1
  • 20
    • 84933021527 scopus 로고
    • Alkoholische Gährung ohne Hefezellen
    • Buchner E. Alkoholische Gährung ohne Hefezellen. Ber. Dtsch. Chem. Ges. 1897, 30:117-124.
    • (1897) Ber. Dtsch. Chem. Ges. , vol.30 , pp. 117-124
    • Buchner, E.1
  • 21
    • 0017328619 scopus 로고
    • Multiple enzyme purifications from muscle extracts by using affinity elution chromatographic procedures
    • Scopes R.K. Multiple enzyme purifications from muscle extracts by using affinity elution chromatographic procedures. Biochem. J. 1977, 161:265-277.
    • (1977) Biochem. J. , vol.161 , pp. 265-277
    • Scopes, R.K.1
  • 22
    • 0021856395 scopus 로고
    • Studies on cell-free metabolism: ethanol production by a yeast glycolytic system reconstituted from purified enzymes
    • Welch P., Scopes R.K. Studies on cell-free metabolism: ethanol production by a yeast glycolytic system reconstituted from purified enzymes. J. Biotechnol. 1985, 2:257-273.
    • (1985) J. Biotechnol. , vol.2 , pp. 257-273
    • Welch, P.1    Scopes, R.K.2
  • 24
    • 0034234048 scopus 로고    scopus 로고
    • Microencapsulation of microbial cells
    • Park J.K., Chang H.N. Microencapsulation of microbial cells. Biotechnol. Adv. 2000, 18:303-319.
    • (2000) Biotechnol. Adv. , vol.18 , pp. 303-319
    • Park, J.K.1    Chang, H.N.2
  • 25
    • 33747126062 scopus 로고    scopus 로고
    • In situ detoxification and continuous cultivation of dilute-acid hydrolyzate to ethanol by encapsulated S. cerevisiae
    • Talebnia F., Taherzadeh M.J. In situ detoxification and continuous cultivation of dilute-acid hydrolyzate to ethanol by encapsulated S. cerevisiae. J. Biotechnol. 2006, 125:377-384.
    • (2006) J. Biotechnol. , vol.125 , pp. 377-384
    • Talebnia, F.1    Taherzadeh, M.J.2
  • 26
    • 84880798904 scopus 로고    scopus 로고
    • Loofah sponge activated by periodate oxidation as a carrier for covalent immobilization of lipase
    • Gong R., Zhang J., Zhu J., Wang J., Lai Q., Jiang B. Loofah sponge activated by periodate oxidation as a carrier for covalent immobilization of lipase. Korean J. Chem. Eng. 2013, 30:1620-1625.
    • (2013) Korean J. Chem. Eng. , vol.30 , pp. 1620-1625
    • Gong, R.1    Zhang, J.2    Zhu, J.3    Wang, J.4    Lai, Q.5    Jiang, B.6
  • 27
    • 0002034250 scopus 로고
    • Encapsulation of food ingredients: a review of available technology, focusing on hydrocolloids
    • S.J. Risch, G.A. Reineccius (Eds.)
    • King A.H. Encapsulation of food ingredients: a review of available technology, focusing on hydrocolloids. Encapsulation and Controlled Release of Food Ingredients, ACS Symposium Series 590 1995, 26-39. S.J. Risch, G.A. Reineccius (Eds.).
    • (1995) Encapsulation and Controlled Release of Food Ingredients, ACS Symposium Series 590 , pp. 26-39
    • King, A.H.1
  • 28
    • 0030297790 scopus 로고    scopus 로고
    • Encapsulation of Lactobacillus casei cells in liquid-core alginate capsules for lactic acid production
    • Yoo I.K., Seong G.H., Chang H.N., Park J.K. Encapsulation of Lactobacillus casei cells in liquid-core alginate capsules for lactic acid production. Enzyme Microb. Technol. 1996, 19:426-433.
    • (1996) Enzyme Microb. Technol. , vol.19 , pp. 426-433
    • Yoo, I.K.1    Seong, G.H.2    Chang, H.N.3    Park, J.K.4
  • 29
    • 0345869798 scopus 로고    scopus 로고
    • Enzyme immobilization in novel alginate-chitosan core-shell microcapsules
    • Taqieddin E., Amiji M. Enzyme immobilization in novel alginate-chitosan core-shell microcapsules. Biomaterials 2004, 25:1937-1945.
    • (2004) Biomaterials , vol.25 , pp. 1937-1945
    • Taqieddin, E.1    Amiji, M.2
  • 30
    • 84861639989 scopus 로고    scopus 로고
    • Nanoreinforced bacterial cellulose-montmorillonite composites for biomedical applications
    • Ul-Islam M., Khan T., Park J.K. Nanoreinforced bacterial cellulose-montmorillonite composites for biomedical applications. Carbohyd. Polym. 2012, 89:1189-1197.
    • (2012) Carbohyd. Polym. , vol.89 , pp. 1189-1197
    • Ul-Islam, M.1    Khan, T.2    Park, J.K.3
  • 31
    • 0029064359 scopus 로고
    • Permeability and blood compatibility properties of chitosan-poly(ethylene oxide) blend membranes for hemodialysis
    • Amiji M.M. Permeability and blood compatibility properties of chitosan-poly(ethylene oxide) blend membranes for hemodialysis. Biomaterials 1995, 16:593-599.
    • (1995) Biomaterials , vol.16 , pp. 593-599
    • Amiji, M.M.1
  • 32
    • 0000360815 scopus 로고
    • A novel immobilization method for prevention of cell leakage from the Gel matrix
    • Tanaka H., Irie S., Ochi H. A novel immobilization method for prevention of cell leakage from the Gel matrix. J. Ferment. Bioeng. 1989, 68:216-219.
    • (1989) J. Ferment. Bioeng. , vol.68 , pp. 216-219
    • Tanaka, H.1    Irie, S.2    Ochi, H.3
  • 33
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 7:248-254.
    • (1976) Anal. Biochem. , vol.7 , pp. 248-254
    • Bradford, M.M.1
  • 34
    • 84907362629 scopus 로고    scopus 로고
    • Quantitative isolation of starch from corn kernels without degradation
    • James P.M., Stig R.E. Quantitative isolation of starch from corn kernels without degradation. Starch-Stärke 2006, 11:342-346.
    • (2006) Starch-Stärke , vol.11 , pp. 342-346
    • James, P.M.1    Stig, R.E.2
  • 35
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller G.L. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 1959, 31:426-428.
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 36
    • 79960603147 scopus 로고    scopus 로고
    • Potential of the waste from beer fermentation broth for bioethanol production without any additional enzyme, microbial cells and carbohydrates
    • Ha J.H., Shah N., Ul-Islam M., Park J.K. Potential of the waste from beer fermentation broth for bioethanol production without any additional enzyme, microbial cells and carbohydrates. Enzyme Microb. Technol. 2011, 49:298-304.
    • (2011) Enzyme Microb. Technol. , vol.49 , pp. 298-304
    • Ha, J.H.1    Shah, N.2    Ul-Islam, M.3    Park, J.K.4
  • 37
    • 25644438460 scopus 로고    scopus 로고
    • Simultaneous saccharification and fermentation of potato starch wastewater to lactic acid by Rhizopus oryzae and Rhizopus arrhizus
    • Huang L.P., Jina B., Lant P., Shou J. Simultaneous saccharification and fermentation of potato starch wastewater to lactic acid by Rhizopus oryzae and Rhizopus arrhizus. Biochem. Eng. J. 2005, 23:265-276.
    • (2005) Biochem. Eng. J. , vol.23 , pp. 265-276
    • Huang, L.P.1    Jina, B.2    Lant, P.3    Shou, J.4
  • 38
    • 84862831797 scopus 로고    scopus 로고
    • Constructing the electricitycarbohydrate-hydrogen cycle for a sustainability revolution
    • Zhang Y.H., Huang W.D. Constructing the electricitycarbohydrate-hydrogen cycle for a sustainability revolution. Trends Biotechnol. 2012, 30:301-306.
    • (2012) Trends Biotechnol. , vol.30 , pp. 301-306
    • Zhang, Y.H.1    Huang, W.D.2
  • 39
    • 79955065138 scopus 로고    scopus 로고
    • Optimization of a blueprint for in vitro glycolysis bymetabolic real-time analysis
    • Bujara M., Schumperli M., Pellaux R., Heinemann M., Panke S. Optimization of a blueprint for in vitro glycolysis bymetabolic real-time analysis. Nat. Chem. Biol. 2011, 7:271-277.
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 271-277
    • Bujara, M.1    Schumperli, M.2    Pellaux, R.3    Heinemann, M.4    Panke, S.5
  • 40
    • 0021792109 scopus 로고
    • Studies on cell-free metabolism: ethanol production by extracts of Zymomonas mobilis
    • Algar E.M., Scopes R.K. Studies on cell-free metabolism: ethanol production by extracts of Zymomonas mobilis. J. Biotechnol. 1985, 2:275-287.
    • (1985) J. Biotechnol. , vol.2 , pp. 275-287
    • Algar, E.M.1    Scopes, R.K.2
  • 42
    • 29244470172 scopus 로고    scopus 로고
    • Immobilization of 2-amylase Produced by Bacillus circulans GRS 313
    • Dey G., Singh B., Banerjee R. Immobilization of 2-amylase Produced by Bacillus circulans GRS 313. Braz. Arch. Biol. Technol. 2003, 46:167-176.
    • (2003) Braz. Arch. Biol. Technol. , vol.46 , pp. 167-176
    • Dey, G.1    Singh, B.2    Banerjee, R.3
  • 43
    • 0027130982 scopus 로고
    • Microencapsulation of yeast cells in the calcium alginate membrane
    • Cheong S.H., Park J.K., Kim B.S., Chang H.N. Microencapsulation of yeast cells in the calcium alginate membrane. Biotechnol. Tech. 1993, 7:879-884.
    • (1993) Biotechnol. Tech. , vol.7 , pp. 879-884
    • Cheong, S.H.1    Park, J.K.2    Kim, B.S.3    Chang, H.N.4
  • 44
    • 15844405967 scopus 로고    scopus 로고
    • Microencapsulation of recombinant Saccharomyces cerevisiae cells with invertase activity in liquid-core alginate capsules
    • Chang H.N., Seong G.H., Yoo I.K., Park J.K., Seo J.H. Microencapsulation of recombinant Saccharomyces cerevisiae cells with invertase activity in liquid-core alginate capsules. Biotechnol. Bioeng. 1996, 51:157-162.
    • (1996) Biotechnol. Bioeng. , vol.51 , pp. 157-162
    • Chang, H.N.1    Seong, G.H.2    Yoo, I.K.3    Park, J.K.4    Seo, J.H.5
  • 45
    • 18844471075 scopus 로고    scopus 로고
    • Glucose oxidase release from calcium alginate gel capsules
    • Blandino A., Macias M., Cantero D. Glucose oxidase release from calcium alginate gel capsules. Enzyme Microb. Technol. 2000, 27:319-324.
    • (2000) Enzyme Microb. Technol. , vol.27 , pp. 319-324
    • Blandino, A.1    Macias, M.2    Cantero, D.3
  • 47
    • 0020944175 scopus 로고
    • Shape and stability of a liquid drop moving at low Weber numbers
    • Frankel I., Weihs D. Shape and stability of a liquid drop moving at low Weber numbers. Appl. Sci. Res. 1983, 40:279-294.
    • (1983) Appl. Sci. Res. , vol.40 , pp. 279-294
    • Frankel, I.1    Weihs, D.2
  • 49
    • 0016802949 scopus 로고
    • The contents of adenine nucleotides, phosphagens and some glycolytic intermediates in resting muscles from vertebrates and invertebrates
    • Beis I., Newsholme E.A. The contents of adenine nucleotides, phosphagens and some glycolytic intermediates in resting muscles from vertebrates and invertebrates. Biochem. J. 1975, 152:23-32.
    • (1975) Biochem. J. , vol.152 , pp. 23-32
    • Beis, I.1    Newsholme, E.A.2
  • 50
    • 0004053611 scopus 로고    scopus 로고
    • John Wiley & Sons Incorporation, New York, NY
    • Voet D., Voet J.G. Biochemistry 2004, John Wiley & Sons Incorporation, New York, NY. third ed.
    • (2004) Biochemistry
    • Voet, D.1    Voet, J.G.2
  • 51
    • 0025728058 scopus 로고
    • Starch hydrolysis kinetics of Bacillus licheniformis α-amylase
    • Komolprasert V., Ofoli R.Y. Starch hydrolysis kinetics of Bacillus licheniformis α-amylase. J. Chem. Technol. Biotechnol. 1991, 51:209-223.
    • (1991) J. Chem. Technol. Biotechnol. , vol.51 , pp. 209-223
    • Komolprasert, V.1    Ofoli, R.Y.2
  • 54
    • 84871158926 scopus 로고    scopus 로고
    • Optimization of immobilization of α-amylase in alginate gel and its comparative biochemical studies with free α-amylase
    • Talekar S., Chavare S. Optimization of immobilization of α-amylase in alginate gel and its comparative biochemical studies with free α-amylase. Rec. Res. Sci. Technol. 2012, 4:1-5.
    • (2012) Rec. Res. Sci. Technol. , vol.4 , pp. 1-5
    • Talekar, S.1    Chavare, S.2
  • 55
    • 0034993188 scopus 로고    scopus 로고
    • Immobilization of invertase within calcium alginate gel capsules
    • Tanriseven A., Dogan S. Immobilization of invertase within calcium alginate gel capsules. Process. Biochem. 2001, 36:1081-1083.
    • (2001) Process. Biochem. , vol.36 , pp. 1081-1083
    • Tanriseven, A.1    Dogan, S.2
  • 56
    • 2442677663 scopus 로고    scopus 로고
    • A new intrinsic thermal parameter for enzymes reveals true temperature optima
    • Peterson M.E., Eisenthal R., Danson M.J., Spence A., Daniel R.M. A new intrinsic thermal parameter for enzymes reveals true temperature optima. J. Biol. Chem. 2004, 279:20717-20722.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20717-20722
    • Peterson, M.E.1    Eisenthal, R.2    Danson, M.J.3    Spence, A.4    Daniel, R.M.5
  • 57
    • 0347646637 scopus 로고    scopus 로고
    • Nanoflow LC Q-TOF MS for De novo peptide sequencing in microbial proteomics
    • Devreese B., Van B.J. Nanoflow LC Q-TOF MS for De novo peptide sequencing in microbial proteomics. LC-GC Eur. 2002, 15:658-662.
    • (2002) LC-GC Eur. , vol.15 , pp. 658-662
    • Devreese, B.1    Van, B.J.2
  • 58
    • 84891345926 scopus 로고    scopus 로고
    • Immobilization of Candida sp. 99-125 lipase onto silanized SBA-15 mesoporous materials by physical adsorption
    • Li Y., Wang W., Han P. Immobilization of Candida sp. 99-125 lipase onto silanized SBA-15 mesoporous materials by physical adsorption. Korean J. Chem. Eng. 2014, 31:98-103.
    • (2014) Korean J. Chem. Eng. , vol.31 , pp. 98-103
    • Li, Y.1    Wang, W.2    Han, P.3
  • 59
    • 84866746381 scopus 로고    scopus 로고
    • Ethanol production by repeated-batch simultaneous saccharification and fermentation (SSF) of alkali-treated rice straw using immobilized Saccharomyces cerevisiae cells
    • Watanabe I., Miyata N., Ando A., Shiroma R., Tokuyasu K., Nakamura T. Ethanol production by repeated-batch simultaneous saccharification and fermentation (SSF) of alkali-treated rice straw using immobilized Saccharomyces cerevisiae cells. Bioresour. Technol. 2012, 123:695-698.
    • (2012) Bioresour. Technol. , vol.123 , pp. 695-698
    • Watanabe, I.1    Miyata, N.2    Ando, A.3    Shiroma, R.4    Tokuyasu, K.5    Nakamura, T.6
  • 60
    • 80052896372 scopus 로고    scopus 로고
    • Ethanol production at elevated temperatures using encapsulation of yeast
    • Ylitervoa P., Franzén C.J., Taherzadeh M.J. Ethanol production at elevated temperatures using encapsulation of yeast. J. Biotechnol. 2011, 156:22-29.
    • (2011) J. Biotechnol. , vol.156 , pp. 22-29
    • Ylitervoa, P.1    Franzén, C.J.2    Taherzadeh, M.J.3
  • 61
    • 0014959635 scopus 로고
    • Characterization of porcine pancreatic isoamylases chemical and physical studies
    • Cozzone P.L., Beaupoil P.B., Mouren G.M. Characterization of porcine pancreatic isoamylases chemical and physical studies. Biochim. Biophys. Acta 1970, 207:490-504.
    • (1970) Biochim. Biophys. Acta , vol.207 , pp. 490-504
    • Cozzone, P.L.1    Beaupoil, P.B.2    Mouren, G.M.3
  • 62
    • 0028446011 scopus 로고
    • Expression in Escherichia coli of cDNA encoding barley β-amylase and properties of recombinant β-amylase
    • Yoshigi N., Okada Y., Sahara H., Koshino S. Expression in Escherichia coli of cDNA encoding barley β-amylase and properties of recombinant β-amylase. Biosci. Biotechnol., Biochem. 1994, 58:1080-1086.
    • (1994) Biosci. Biotechnol., Biochem. , vol.58 , pp. 1080-1086
    • Yoshigi, N.1    Okada, Y.2    Sahara, H.3    Koshino, S.4
  • 63
    • 0015493834 scopus 로고
    • Purification and characterisation of crystalline β-amylase from Barley
    • Visuri K., Nummi M. Purification and characterisation of crystalline β-amylase from Barley. Eur. J. Biochem. 1972, 28:555-585.
    • (1972) Eur. J. Biochem. , vol.28 , pp. 555-585
    • Visuri, K.1    Nummi, M.2
  • 64
    • 0029012960 scopus 로고
    • Biochemical and molecular characterization of a barley seed β-glucosidase
    • Leah R., Kigel J., Svendsen I., Mundy J. Biochemical and molecular characterization of a barley seed β-glucosidase. J. Biol. Chem. 1995, 26:15789-15797.
    • (1995) J. Biol. Chem. , vol.26 , pp. 15789-15797
    • Leah, R.1    Kigel, J.2    Svendsen, I.3    Mundy, J.4
  • 65
    • 0017333187 scopus 로고
    • Studies on almond emulsin β-d-glucosidase I. Isolation and characterization of a bifunctional isozyme
    • Grover A.K., Macmurchie D.D., Cushley R.J. Studies on almond emulsin β-d-glucosidase I. Isolation and characterization of a bifunctional isozyme. Biochim. Biophys. Acta 1977, 482:98-108.
    • (1977) Biochim. Biophys. Acta , vol.482 , pp. 98-108
    • Grover, A.K.1    Macmurchie, D.D.2    Cushley, R.J.3
  • 66
    • 0022633064 scopus 로고
    • Extracellular Pullulanase of Klebsiella pneumoniae is a lipoprotein
    • Pugsley A.P., Chapon C., Schwartz M. Extracellular Pullulanase of Klebsiella pneumoniae is a lipoprotein. J. Bacteriol. 1986, 166:1083-1088.
    • (1986) J. Bacteriol. , vol.166 , pp. 1083-1088
    • Pugsley, A.P.1    Chapon, C.2    Schwartz, M.3


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