메뉴 건너뛰기




Volumn 176, Issue 6, 2015, Pages 1564-1580

A NaBH4 Coupled Ninhydrin-Based Assay for the Quantification of Protein/Enzymes During the Enzymatic Hydrolysis of Pretreated Lignocellulosic Biomass

Author keywords

Cellulase enzymes; Enzymatic hydrolysis; Lignocellulose; Ninhydrin; Protein quantification

Indexed keywords

ASSAYS; BIOMASS; ENZYME KINETICS; SODIUM BOROHYDRIDE;

EID: 84937969878     PISSN: 02732289     EISSN: 15590291     Source Type: Journal    
DOI: 10.1007/s12010-015-1662-7     Document Type: Article
Times cited : (23)

References (35)
  • 2
    • 84900423262 scopus 로고    scopus 로고
    • Process design and economics for the conversion of lignocellulosic biomass to hydrocarbons: dilute-acid and enzymatic deconstruction of biomass to sugars and biological conversion of sugars to hydrocarbons. Technical report
    • Golden: CO
    • Davis, R., Tao, L., Tan, E.C.D., Biddy, M.J., Beckham, G.T., Scarlata, C., et al. (2013). Process design and economics for the conversion of lignocellulosic biomass to hydrocarbons: dilute-acid and enzymatic deconstruction of biomass to sugars and biological conversion of sugars to hydrocarbons. Technical report, National Renewable Energy Laboratory. Golden, CO.
    • (2013) National Renewable Energy Laboratory
    • Davis, R.1    Tao, L.2    Tan, E.C.D.3    Biddy, M.J.4    Beckham, G.T.5    Scarlata, C.6
  • 3
    • 84655169446 scopus 로고    scopus 로고
    • Process design and economics for biochemical conversion of lignocellulosic biomass to ethanol: dilute-acid pretreatment and enzymatic hydrolysis of corn stover. Technical report
    • Golden: CO
    • Humbird, D., Davis, R., Tao, L., Kinchin, C., Hsu, D., Aden, A., et al. (2011). Process design and economics for biochemical conversion of lignocellulosic biomass to ethanol: dilute-acid pretreatment and enzymatic hydrolysis of corn stover. Technical report, National Renewable Energy Laboratory. Golden, CO.
    • (2011) National Renewable Energy Laboratory
    • Humbird, D.1    Davis, R.2    Tao, L.3    Kinchin, C.4    Hsu, D.5    Aden, A.6
  • 4
    • 84943470296 scopus 로고
    • Measurement of cellulase activities
    • COI: 1:CAS:528:DyaL2sXpvVeltA%3D%3D
    • Ghose, T. K. (1987). Measurement of cellulase activities. Pure and Applied Chemistry, 59, 257–268.
    • (1987) Pure and Applied Chemistry , vol.59 , pp. 257-268
    • Ghose, T.K.1
  • 6
    • 79751535329 scopus 로고    scopus 로고
    • Cellulose accessibility limits the effectiveness of minimum cellulase loading on the efficient hydrolysis of pretreated lignocellulosic substrates
    • COI: 1:CAS:528:DC%2BC3MXjt1Khsr8%3D
    • Arantes, V., & Saddler, J. N. (2011). Cellulose accessibility limits the effectiveness of minimum cellulase loading on the efficient hydrolysis of pretreated lignocellulosic substrates. Biotechnology for Biofuels, 4, 3.
    • (2011) Biotechnology for Biofuels , vol.4 , pp. 3
    • Arantes, V.1    Saddler, J.N.2
  • 7
    • 80052607331 scopus 로고    scopus 로고
    • Comparative performance of precommercial cellulases hydrolyzing pretreated corn stover
    • COI: 1:CAS:528:DC%2BC3MXht12ns77I
    • McMillan, J. D., Jennings, E. W., Mohagheghi, A., & Zuccarello, M. (2011). Comparative performance of precommercial cellulases hydrolyzing pretreated corn stover. Biotechnology for Biofuels, 4, 29.
    • (2011) Biotechnology for Biofuels , vol.4 , pp. 29
    • McMillan, J.D.1    Jennings, E.W.2    Mohagheghi, A.3    Zuccarello, M.4
  • 12
    • 10844286172 scopus 로고    scopus 로고
    • Toward an aggregated understanding of enzymatic hydrolysis of cellulose: noncomplexed cellulase systems
    • COI: 1:CAS:528:DC%2BD2cXhtVOitrjE
    • Zhang, Y. H., & Lynd, L. R. (2004). Toward an aggregated understanding of enzymatic hydrolysis of cellulose: noncomplexed cellulase systems. Biotechnology and Bioengineering, 88, 797–824.
    • (2004) Biotechnology and Bioengineering , vol.88 , pp. 797-824
    • Zhang, Y.H.1    Lynd, L.R.2
  • 13
    • 33751248467 scopus 로고    scopus 로고
    • 2+-reduction by phenol derivatives associated with Azure B degradation in Fenton-like reactions
    • COI: 1:CAS:528:DC%2BD28Xht1CqtL3O
    • 2+-reduction by phenol derivatives associated with Azure B degradation in Fenton-like reactions. Chemosphere, 66, 947–954.
    • (2007) Chemosphere , vol.66 , pp. 947-954
    • Aguiar, A.1    Ferraz, A.2
  • 14
    • 0025063651 scopus 로고
    • Determination of soluble lignin and proteins in the presence of each other
    • COI: 1:CAS:528:DyaK3cXlslChu7c%3D
    • Chauvet, J., & Lamy, F. (1990). Determination of soluble lignin and proteins in the presence of each other. Analytica Chimica Acta, 235, 299–306.
    • (1990) Analytica Chimica Acta , vol.235 , pp. 299-306
    • Chauvet, J.1    Lamy, F.2
  • 15
    • 84864386570 scopus 로고    scopus 로고
    • Precipitation of Trichoderma reesei commercial cellulase preparations under standard enzymatic hydrolysis conditions for lignocelluloses
    • COI: 1:CAS:528:DC%2BC38XhtVyks77F
    • Chylenski, P., Felby, C., Ostergaard, H. M., Gama, M., & Selig, M. J. (2012). Precipitation of Trichoderma reesei commercial cellulase preparations under standard enzymatic hydrolysis conditions for lignocelluloses. Biotechnology Letters, 34, 1475–1482.
    • (2012) Biotechnology Letters , vol.34 , pp. 1475-1482
    • Chylenski, P.1    Felby, C.2    Ostergaard, H.M.3    Gama, M.4    Selig, M.J.5
  • 16
    • 0001247395 scopus 로고
    • On phosphotungstic-phosphomolybdic compounds as color reagents
    • COI: 1:CAS:528:DyaC38XisVCktQ%3D%3D
    • Folin, O., & Denis, W. (1912). On phosphotungstic-phosphomolybdic compounds as color reagents. Journal of Biological Chemistry, 12, 239–243.
    • (1912) Journal of Biological Chemistry , vol.12 , pp. 239-243
    • Folin, O.1    Denis, W.2
  • 17
    • 0034233432 scopus 로고    scopus 로고
    • Use of UV absorbance to monitor furans in dilute acid hydrolysates of biomass
    • COI: 1:CAS:528:DC%2BD3cXksFGrsL0%3D
    • Martinez, A., Rodriguez, M. E., York, S. W., Preston, J. F., & Ingram, L. O. (2000). Use of UV absorbance to monitor furans in dilute acid hydrolysates of biomass. Biotechnology Progress, 16, 637–641.
    • (2000) Biotechnology Progress , vol.16 , pp. 637-641
    • Martinez, A.1    Rodriguez, M.E.2    York, S.W.3    Preston, J.F.4    Ingram, L.O.5
  • 18
    • 84937989075 scopus 로고
    • Some factors causing colour in acetate pulp and cellulose acetate
    • Turunen, J., & Turunen, K. (1967). Some factors causing colour in acetate pulp and cellulose acetate. Pure and Applied Chemistry, 67, 555–562.
    • (1967) Pure and Applied Chemistry , vol.67 , pp. 555-562
    • Turunen, J.1    Turunen, K.2
  • 21
    • 0842284714 scopus 로고    scopus 로고
    • Applications of the ninhydrin reaction for analysis of amino acids, peptides, and proteins to agricultural and biomedical sciences
    • COI: 1:CAS:528:DC%2BD2cXjtFWqsA%3D%3D
    • Friedman, M. (2004). Applications of the ninhydrin reaction for analysis of amino acids, peptides, and proteins to agricultural and biomedical sciences. Journal of Agricultural and Food Chemistry, 52, 385–406.
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , pp. 385-406
    • Friedman, M.1
  • 22
    • 79251508897 scopus 로고    scopus 로고
    • Determination of in-gel protein concentration by a ninhydrin-based method
    • COI: 1:CAS:528:DC%2BC3MXpvVCisg%3D%3D
    • Kang, S. U., & Lubec, G. (2011). Determination of in-gel protein concentration by a ninhydrin-based method. Proteomics, 11, 481–484.
    • (2011) Proteomics , vol.11 , pp. 481-484
    • Kang, S.U.1    Lubec, G.2
  • 23
    • 0022426044 scopus 로고
    • Measurement of total protein in plant samples in the presence of tannins
    • COI: 1:CAS:528:DyaL2MXitFOktrY%3D
    • Marks, D. L., Buchsbaum, R., & Swain, T. (1985). Measurement of total protein in plant samples in the presence of tannins. Analytical Biochemistry, 147, 136–143.
    • (1985) Analytical Biochemistry , vol.147 , pp. 136-143
    • Marks, D.L.1    Buchsbaum, R.2    Swain, T.3
  • 24
    • 0035339420 scopus 로고    scopus 로고
    • A ninhydrin-based assay to quantitate the total protein content of tissue samples
    • COI: 1:CAS:528:DC%2BD3MXivFalu70%3D
    • Starcher, B. (2001). A ninhydrin-based assay to quantitate the total protein content of tissue samples. Analytical Biochemistry, 292, 125–129.
    • (2001) Analytical Biochemistry , vol.292 , pp. 125-129
    • Starcher, B.1
  • 25
    • 84894465631 scopus 로고    scopus 로고
    • The challenging measurement of protein in complex biomass-derived samples
    • Haven, M. O., & Jorgensen, H. (2013). The challenging measurement of protein in complex biomass-derived samples. Applied Biochemistry and Biotechnology, 172, 1–15.
    • (2013) Applied Biochemistry and Biotechnology , vol.172
    • Haven, M.O.1    Jorgensen, H.2
  • 27
    • 0031784879 scopus 로고    scopus 로고
    • Hydrolysis and amino acid composition analysis of proteins
    • COI: 1:CAS:528:DyaK1MXjsFah
    • Fountoulakis, M., & Lahm, H. (1998). Hydrolysis and amino acid composition analysis of proteins. Journal of Chromatography A, 826, 109–134.
    • (1998) Journal of Chromatography A , vol.826 , pp. 109-134
    • Fountoulakis, M.1    Lahm, H.2
  • 29
    • 33749001258 scopus 로고    scopus 로고
    • Determination of sugars, byproducts, and degradation products in liquid fraction process samples. Technical report
    • Golden: CO
    • Sluiter, A., Hames, B., Ruiz, R., Scarlata, C., Sluiter, J. and Templeton, D. (2006). Determination of sugars, byproducts, and degradation products in liquid fraction process samples. Technical report, National Renewable Energy Laboratory. Golden, CO.
    • (2006) National Renewable Energy Laboratory
    • Sluiter, A.1    Hames, B.2    Ruiz, R.3    Scarlata, C.4    Sluiter, J.5    Templeton, D.6
  • 30
    • 33845388161 scopus 로고    scopus 로고
    • A simple 96-well microplate method for estimation of total polyphenol content in seaweeds
    • COI: 1:CAS:528:DC%2BD28Xht1KmtrvO
    • Zhang, Q., Zhang, J., Shen, J., Silva, A., Dennis, D., & Barrow, C. (2006). A simple 96-well microplate method for estimation of total polyphenol content in seaweeds. Journal of Applied Phycology, 18, 445–450.
    • (2006) Journal of Applied Phycology , vol.18 , pp. 445-450
    • Zhang, Q.1    Zhang, J.2    Shen, J.3    Silva, A.4    Dennis, D.5    Barrow, C.6
  • 31
    • 0022493894 scopus 로고
    • 14C]cellobiose with clostridium thermocellum cellobiose phosphorylase
    • COI: 1:CAS:528:DyaL2sXmtl2ltQ%3D%3D
    • 14C]cellobiose with clostridium thermocellum cellobiose phosphorylase. Applied and Environmental Microbiology, 52, 902–904.
    • (1986) Applied and Environmental Microbiology , vol.52 , pp. 902-904
    • Ng, T.K.1    Zeikus, J.G.2
  • 32
    • 72549085335 scopus 로고    scopus 로고
    • Direct quantitative determination of adsorbed cellulase on lignocellulosic biomass with its application to study cellulase desorption for potential recycling
    • COI: 1:CAS:528:DC%2BD1MXht1Ortb%2FE
    • Zhu, Z., Sathitsuksanoh, N., & Percival Zhang, Y. H. (2009). Direct quantitative determination of adsorbed cellulase on lignocellulosic biomass with its application to study cellulase desorption for potential recycling. Analyst, 134, 2267–2272.
    • (2009) Analyst , vol.134 , pp. 2267-2272
    • Zhu, Z.1    Sathitsuksanoh, N.2    Percival Zhang, Y.H.3
  • 33
    • 0036843468 scopus 로고    scopus 로고
    • Adsorption properties of the fibril forming protein from Trichoderma reesei
    • COI: 1:CAS:528:DC%2BD38Xns1aksLo%3D
    • Banka, R. R., & Mishra, S. (2002). Adsorption properties of the fibril forming protein from Trichoderma reesei. Enzyme and Microbial Technology, 31, 784–793.
    • (2002) Enzyme and Microbial Technology , vol.31 , pp. 784-793
    • Banka, R.R.1    Mishra, S.2
  • 35
    • 71549152820 scopus 로고    scopus 로고
    • Quantitation of protein
    • COI: 1:CAS:528:DC%2BC3cXmt12jsg%3D%3D
    • Noble, J. E., & Bailey, M. J. (2009). Quantitation of protein. Methods in Enzymology, 463, 73–95.
    • (2009) Methods in Enzymology , vol.463 , pp. 73-95
    • Noble, J.E.1    Bailey, M.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.