메뉴 건너뛰기




Volumn 188, Issue , 2015, Pages 201-209

Circular dichroism and infrared spectroscopic characterization of secondary structure components of protein Z during mashing and boiling processes

Author keywords

CD; FTIR; Mashing and boiling processes; Protein Z; Secondary structure

Indexed keywords

AMINO ACIDS; BEER; BREWING; CHEMICAL RESISTANCE; CIRCULAR DICHROISM SPECTROSCOPY; DICHROISM; FERMENTATION; FOURIER TRANSFORM INFRARED SPECTROSCOPY;

EID: 84928946866     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2015.04.053     Document Type: Article
Times cited : (66)

References (39)
  • 2
    • 14944340300 scopus 로고    scopus 로고
    • The relative significance of physics and chemistry for beer foam excellence: Theory and practice
    • C. Bamforth The relative significance of physics and chemistry for beer foam excellence: Theory and practice Journal of the Institute of Brewing 110 4 2004 259 266
    • (2004) Journal of the Institute of Brewing , vol.110 , Issue.4 , pp. 259-266
    • Bamforth, C.1
  • 4
    • 34547849614 scopus 로고    scopus 로고
    • Proteomic identification of technologically modified proteins in malt by combination of protein fractionation using convective interaction media and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • J. Bobalova, and J. Chmelik Proteomic identification of technologically modified proteins in malt by combination of protein fractionation using convective interaction media and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry Journal of Chromatography A 1163 1 2007 80 85
    • (2007) Journal of Chromatography A , vol.1163 , Issue.1 , pp. 80-85
    • Bobalova, J.1    Chmelik, J.2
  • 6
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • D.M. Byler, and H. Susi Examination of the secondary structure of proteins by deconvolved FTIR spectra Biopolymers 25 3 1986 469 487
    • (1986) Biopolymers , vol.25 , Issue.3 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 9
    • 0033450813 scopus 로고    scopus 로고
    • The impact of malt derived proteins on beer foam quality. Part II: The influence of malt foam-positive proteins and non-starch polysaccharides on beer foam quality
    • D.E. Evans, M. Sheehan, and D. Stewart The impact of malt derived proteins on beer foam quality. Part II: The influence of malt foam-positive proteins and non-starch polysaccharides on beer foam quality Journal of the Institute of Brewing 105 3 1999 171 178
    • (1999) Journal of the Institute of Brewing , vol.105 , Issue.3 , pp. 171-178
    • Evans, D.E.1    Sheehan, M.2    Stewart, D.3
  • 11
    • 78649336731 scopus 로고    scopus 로고
    • Barley for brewing: Characteristic changes during malting, brewing and applications of its by-products
    • M. Gupta, N. Abu-Ghannam, and E. Gallaghar Barley for brewing: Characteristic changes during malting, brewing and applications of its by-products Comprehensive Reviews in Food Science and Food Safety 9 3 2010 318 328
    • (2010) Comprehensive Reviews in Food Science and Food Safety , vol.9 , Issue.3 , pp. 318-328
    • Gupta, M.1    Abu-Ghannam, N.2    Gallaghar, E.3
  • 12
    • 84979403918 scopus 로고
    • Gene products of barley chromosomes 4 and 7 are precursors of the major antigenic beer protein
    • J. Hejgaard Gene products of barley chromosomes 4 and 7 are precursors of the major antigenic beer protein Journal of the Institute of Brewing 90 2 1984 85 87
    • (1984) Journal of the Institute of Brewing , vol.90 , Issue.2 , pp. 85-87
    • Hejgaard, J.1
  • 13
    • 84979404818 scopus 로고
    • Purification and properties of the major antigenic beer protein of barley origin
    • J. Hejgaard, and P. Kaersgaard Purification and properties of the major antigenic beer protein of barley origin Journal of the Institute of Brewing 89 6 1983 402 410
    • (1983) Journal of the Institute of Brewing , vol.89 , Issue.6 , pp. 402-410
    • Hejgaard, J.1    Kaersgaard, P.2
  • 14
    • 0001813953 scopus 로고
    • Sequence homology between barley endosperm protein Z and protease inhibitors of the α 1-antitrypsin family
    • J. Hejgaard, S. Rasmussen, A. Brandt, and I. Svendsen Sequence homology between barley endosperm protein Z and protease inhibitors of the α 1-antitrypsin family FEBS Letters 180 1 1985 89 94
    • (1985) FEBS Letters , vol.180 , Issue.1 , pp. 89-94
    • Hejgaard, J.1    Rasmussen, S.2    Brandt, A.3    Svendsen, I.4
  • 18
    • 0002336495 scopus 로고
    • Biomembrane structure from FT-IR spectroscopy
    • M. Jackson, and H. Mantsch Biomembrane structure from FT-IR spectroscopy Spectrochimica Acta Reviews 15 1 1993 53 69
    • (1993) Spectrochimica Acta Reviews , vol.15 , Issue.1 , pp. 53-69
    • Jackson, M.1    Mantsch, H.2
  • 19
    • 84872594118 scopus 로고    scopus 로고
    • Proteome analysis of metabolic proteins (p i 4-7) in barley (Hordeum vulgare) malts and initial application in malt quality discrimination
    • Z. Jin, Y.-W. Mu, J.-Y. Sun, X.-M. Li, X.-L. Gao, and J. Lu Proteome analysis of metabolic proteins (p I 4-7) in barley (Hordeum vulgare) malts and initial application in malt quality discrimination Journal of Agricultural and Food Chemistry 61 2 2012 402 409
    • (2012) Journal of Agricultural and Food Chemistry , vol.61 , Issue.2 , pp. 402-409
    • Jin, Z.1    Mu, Y.-W.2    Sun, J.-Y.3    Li, X.-M.4    Gao, X.-L.5    Lu, J.6
  • 21
    • 0000337013 scopus 로고
    • Fourier self-deconvolution: A method for resolving intrinsically overlapped bands
    • J.K. Kauppinen, D.J. Moffatt, H.H. Mantsch, and D.G. Cameron Fourier self-deconvolution: A method for resolving intrinsically overlapped bands Applied Spectroscopy 35 3 1981 271 276
    • (1981) Applied Spectroscopy , vol.35 , Issue.3 , pp. 271-276
    • Kauppinen, J.K.1    Moffatt, D.J.2    Mantsch, H.H.3    Cameron, D.G.4
  • 22
    • 0000026399 scopus 로고
    • Effect of disulfide bond cleavage on structural and interfacial properties of whey proteins
    • N.K. Kella, S.T. Yang, and J.E. Kinsella Effect of disulfide bond cleavage on structural and interfacial properties of whey proteins Journal of Agricultural and Food Chemistry 37 5 1989 1203 1210
    • (1989) Journal of Agricultural and Food Chemistry , vol.37 , Issue.5 , pp. 1203-1210
    • Kella, N.K.1    Yang, S.T.2    Kinsella, J.E.3
  • 24
    • 84858326785 scopus 로고    scopus 로고
    • Exploration of beer proteome using OFFGEL prefractionation in combination with two-dimensional gel electrophoresis with narrow pH range gradients
    • H. Konečná, L.S. Müller, H. Dosoudilová, D. Potěšil, J. Buršíková, and O. Šedo Exploration of beer proteome using OFFGEL prefractionation in combination with two-dimensional gel electrophoresis with narrow pH range gradients Journal of Agricultural and Food Chemistry 60 10 2012 2418 2426
    • (2012) Journal of Agricultural and Food Chemistry , vol.60 , Issue.10 , pp. 2418-2426
    • Konečná, H.1    Müller, L.S.2    Dosoudilová, H.3    Potěšil, D.4    Buršíková, J.5    Šedo, O.6
  • 25
    • 34548094323 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic analysis of protein secondary structures
    • J. Kong, and S. Yu Fourier transform infrared spectroscopic analysis of protein secondary structures Acta Biochimica et Biophysica Sinica 39 8 2007 549 559
    • (2007) Acta Biochimica et Biophysica Sinica , vol.39 , Issue.8 , pp. 549-559
    • Kong, J.1    Yu, S.2
  • 26
    • 0038047702 scopus 로고    scopus 로고
    • Beer polypeptides and silica gel part II. Polypeptides involved in foam formation
    • K.A. Leiper, G.G. Stewart, and I.P. McKeown Beer polypeptides and silica gel part II. Polypeptides involved in foam formation Journal of the Institute of Brewing 109 1 2003 73 79
    • (2003) Journal of the Institute of Brewing , vol.109 , Issue.1 , pp. 73-79
    • Leiper, K.A.1    Stewart, G.G.2    McKeown, I.P.3
  • 27
    • 0017309766 scopus 로고
    • Structural patterns in globular proteins
    • M. Levitt, and C. Chothia Structural patterns in globular proteins Nature 261 5561 1976 552 558
    • (1976) Nature , vol.261 , Issue.5561 , pp. 552-558
    • Levitt, M.1    Chothia, C.2
  • 30
    • 0034650323 scopus 로고    scopus 로고
    • Spectroscopic methods for analysis of protein secondary structure
    • J.T. Pelton, and L.R. McLean Spectroscopic methods for analysis of protein secondary structure Analytical Biochemistry 277 2 2000 167 176
    • (2000) Analytical Biochemistry , vol.277 , Issue.2 , pp. 167-176
    • Pelton, J.T.1    McLean, L.R.2
  • 31
    • 33646508515 scopus 로고    scopus 로고
    • Stability of barley and malt lipid transfer protein 1 (LTP1) toward heating and reducing agents: Relationships with the brewing process
    • L. Perrocheau, B. Bakan, P. Boivin, and D. Marion Stability of barley and malt lipid transfer protein 1 (LTP1) toward heating and reducing agents: relationships with the brewing process Journal of Agricultural and Food Chemistry 54 8 2006 3108 3113
    • (2006) Journal of Agricultural and Food Chemistry , vol.54 , Issue.8 , pp. 3108-3113
    • Perrocheau, L.1    Bakan, B.2    Boivin, P.3    Marion, D.4
  • 32
    • 0001779141 scopus 로고
    • The role of positive and negative factors in head retention
    • Pierce, J. (1978). The role of positive and negative factors in head retention. In Proceedings of the 15th convention (pp. 51-65).
    • (1978) Proceedings of the 15th Convention , pp. 51-65
    • Pierce, J.1
  • 33
    • 0000772570 scopus 로고
    • Glycoproteins and beer foam
    • Roberts, R. (1975). Glycoproteins and beer foam. In Proc. Eur. Brew. Conv., Vol. 15 (pp. 453-464).
    • (1975) Proc. Eur. Brew. Conv. , vol.15 , pp. 453-464
    • Roberts, R.1
  • 34
    • 0033512695 scopus 로고    scopus 로고
    • Amadori albumin in type 1 diabetic patients: Correlation with markers of endothelial function, association with diabetic nephropathy, and localization in retinal capillaries
    • C.G. Schalkwijk, N. Ligtvoet, H. Twaalfhoven, A. Jager, H. Blaauwgeers, and R. Schlingemann Amadori albumin in type 1 diabetic patients: Correlation with markers of endothelial function, association with diabetic nephropathy, and localization in retinal capillaries Diabetes 48 12 1999 2446 2453
    • (1999) Diabetes , vol.48 , Issue.12 , pp. 2446-2453
    • Schalkwijk, C.G.1    Ligtvoet, N.2    Twaalfhoven, H.3    Jager, A.4    Blaauwgeers, H.5    Schlingemann, R.6
  • 35
    • 0042415651 scopus 로고    scopus 로고
    • Basic aspects of the technique and applications of infrared spectroscopy of peptides and proteins
    • Washington, DC: American Chemical Society, 1999
    • Singh, B. R. (2000). Basic aspects of the technique and applications of infrared spectroscopy of peptides and proteins. In ACS symposium series, vol. 750 (pp. 2-37). Washington, DC: American Chemical Society, 1999.
    • (2000) ACS Symposium Series , vol.750 , pp. 2-37
    • Singh, B.R.1
  • 36
    • 0037302324 scopus 로고    scopus 로고
    • Structural composition of βi- and βiI-proteins
    • N. Sreerama, and R.W. Woody Structural composition of βI- and βII-proteins Protein Science 12 2 2003 384 388
    • (2003) Protein Science , vol.12 , Issue.2 , pp. 384-388
    • Sreerama, N.1    Woody, R.W.2
  • 37
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases
    • L. Whitmore, and B.A. Wallace Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases Biopolymers 89 5 2008 392 400
    • (2008) Biopolymers , vol.89 , Issue.5 , pp. 392-400
    • Whitmore, L.1    Wallace, B.A.2
  • 38
    • 0037343160 scopus 로고    scopus 로고
    • Effects of oligomerization and secondary structure on the surface behavior of pulmonary surfactant proteins SP-B and SP-C
    • N. Wüstneck, R. Wüstneck, J. Perez-Gil, and U. Pison Effects of oligomerization and secondary structure on the surface behavior of pulmonary surfactant proteins SP-B and SP-C Biophysical Journal 84 3 2003 1940 1949
    • (2003) Biophysical Journal , vol.84 , Issue.3 , pp. 1940-1949
    • Wüstneck, N.1    Wüstneck, R.2    Perez-Gil, J.3    Pison, U.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.