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Volumn 60, Issue 17, 2012, Pages 4327-4335

Reactions between β-lactoglobulin and Genipin: Kinetics and characterization of the products

Author keywords

AFM; cross linking reaction; genipin; kinetics; MALDI.TOF mass spectrometry; Lactoglobulin

Indexed keywords

ACTIVATION ENERGY; ALKALINITY; ATOMIC FORCE MICROSCOPY; ELECTROPHORESIS; ENZYME KINETICS; KINETICS; MASS SPECTROMETRY; POLYACRYLATES; REACTION KINETICS; SODIUM DODECYL SULFATE; SULFUR COMPOUNDS;

EID: 84860479841     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf300311k     Document Type: Article
Times cited : (19)

References (55)
  • 1
    • 0015719269 scopus 로고
    • The constituents of Gardenia jasminoides geniposide and genipin-gentiobioside
    • Endo, T.; Taguchi, H. The constituents of Gardenia jasminoides geniposide and genipin-gentiobioside Chem. Pharm. Bull. 1973, 21 (12) 2684-2688
    • (1973) Chem. Pharm. Bull. , vol.21 , Issue.12 , pp. 2684-2688
    • Endo, T.1    Taguchi, H.2
  • 2
    • 0000326480 scopus 로고
    • Naturally occurring oxygen heterocyclics. IX. Isolation and characterization of genipin
    • Djerassi, C.; Gray, J.; Kincl, F. Naturally occurring oxygen heterocyclics. IX. Isolation and characterization of genipin J. Org. Chem. 1960, 25 (12) 2174-2177
    • (1960) J. Org. Chem. , vol.25 , Issue.12 , pp. 2174-2177
    • Djerassi, C.1    Gray, J.2    Kincl, F.3
  • 3
    • 31344449552 scopus 로고    scopus 로고
    • Anti-inflammatory evaluation of gardenia extract, geniposide and genipin
    • DOI 10.1016/j.jep.2005.08.011, PII S0378874105005283
    • Koo, H.; Lim, K.; Jung, H.; Park, E. Anti-inflammatory evaluation of Gardenia extract, geniposide and genipin J. Ethnopharmacol. 2006, 103 (3) 496-500 (Pubitemid 43143390)
    • (2006) Journal of Ethnopharmacology , vol.103 , Issue.3 , pp. 496-500
    • Koo, H.-J.1    Lim, K.-H.2    Jung, H.-J.3    Park, E.-H.4
  • 5
    • 85008728341 scopus 로고
    • Genipin, a new type of protein crosslinking reagent from Gardenia fruits
    • Fujikawa, S.; Nakamura, S.; Koga, K. Genipin, a new type of protein crosslinking reagent from Gardenia fruits Agric. Biol. Chem. 1988, 52 (3) 869-870
    • (1988) Agric. Biol. Chem. , vol.52 , Issue.3 , pp. 869-870
    • Fujikawa, S.1    Nakamura, S.2    Koga, K.3
  • 6
    • 0348252141 scopus 로고    scopus 로고
    • Mechanism and kinetics of the crosslinking reaction between biopolymers containing primary amine groups and genipin
    • DOI 10.1002/pola.10960
    • Butler, M.; Ng, Y.-F.; Pudney, P. Mechanism and kinetics of the crosslinking reaction between biopolymers containing primary amine groups and genipin J. Polym. Sci., Part A: Polym. Chem. 2003, 41 (24) 3941-3953 (Pubitemid 37538677)
    • (2003) Journal of Polymer Science, Part A: Polymer Chemistry , vol.41 , Issue.24 , pp. 3941-3953
    • Butler, M.F.1    Ng, Y.-F.2    Pudney, P.D.A.3
  • 7
    • 77958179941 scopus 로고    scopus 로고
    • Formulation and characterization of silk sericin-PVA scaffold crosslinked with genipin
    • Aramwit, P.; Siritientong, T.; Kanokpanont, S.; Srichana, T. Formulation and characterization of silk sericin-PVA scaffold crosslinked with genipin Int. J. Biol. Macromol. 2010, 47 (5) 668-675
    • (2010) Int. J. Biol. Macromol. , vol.47 , Issue.5 , pp. 668-675
    • Aramwit, P.1    Siritientong, T.2    Kanokpanont, S.3    Srichana, T.4
  • 8
    • 0032534707 scopus 로고    scopus 로고
    • Feasibility study of a natural crosslinking reagent for biological tissue fixation
    • DOI 10.1002/(SICI)1097-4636(19981215)42:4<560::AID-JBM12>3.0.CO;2-I
    • Sung, H.; Huang, R.; Huang, L.; Tsai, C.; Chiu, C. Feasibility study of a natural crosslinking reagent for biological tissue fixation J. Biomed. Mater. Res. 1998, 42 (4) 560-567 (Pubitemid 28503761)
    • (1998) Journal of Biomedical Materials Research , vol.42 , Issue.4 , pp. 560-567
    • Sung, H.-W.1    Huang, R.-N.2    Huang, L.L.H.3    Tsai, C.-C.4    Chiu, C.-T.5
  • 9
    • 0347482466 scopus 로고    scopus 로고
    • Genipin-crosslinked gelatin microspheres as a drug carrier for intramuscular administration: In vitro and in vivo studies
    • Liang, H.; Chang, W.; Lin, K.; Sung, H. Genipin-crosslinked gelatin microspheres as a drug carrier for intramuscular administration: In vitro and in vivo studies J. Biomed. Mater. Res., Part A 2003, 65 (2) 271-282 (Pubitemid 37521434)
    • (2003) Journal of Biomedical Materials Research - Part A , vol.65 , Issue.2 , pp. 271-282
    • Liang, H.-C.1    Chang, W.-H.2    Lin, K.-J.3    Sung, H.-W.4
  • 10
    • 0036010376 scopus 로고    scopus 로고
    • In vivo evaluation of cellular and acellular bovine pericardia fixed with a naturally occurring crosslinking agent (genipin)
    • DOI 10.1016/S0142-9612(01)00379-9, PII S0142961201003799
    • Chang, Y.; Tsai, C.; Liang, H.; Sung, H. In vivo evaluation of cellular and acellular bovine pericardia fixed with a naturally occurring crosslinking agent (genipin) Biomaterials 2002, 23 (12) 2447-2457 (Pubitemid 34288486)
    • (2002) Biomaterials , vol.23 , Issue.12 , pp. 2447-2457
    • Chang, Y.1    Tsai, C.-C.2    Liang, H.-C.3    Sung, H.-W.4
  • 11
    • 70349472900 scopus 로고    scopus 로고
    • Effects of nerve growth factor from genipin-crosslinked gelatin in polycaprolactone conduit on peripheral nerve regeneration - In vitro and in vivo
    • Chang, C. Effects of nerve growth factor from genipin-crosslinked gelatin in polycaprolactone conduit on peripheral nerve regeneration - In vitro and in vivo J. Biomed. Mater. Res., Part A 2009, 91 (2) 586-596
    • (2009) J. Biomed. Mater. Res., Part A , vol.91 , Issue.2 , pp. 586-596
    • Chang, C.1
  • 12
    • 11144320363 scopus 로고    scopus 로고
    • An in vivo evaluation of a biodegradable genipin-cross-linked gelatin peripheral nerve guide conduit material
    • DOI 10.1016/j.biomaterials.2004.09.060, PII S0142961204008877
    • Chen, Y.; Chang, J.; Cheng, C.; Tsai, F.; Yao, C.; Liu, B. An in vivo evaluation of a biodegradable genipin-cross-linked gelatin peripheral nerve guide conduit material Biomaterials 2005, 26 (18) 3911-3918 (Pubitemid 40038782)
    • (2005) Biomaterials , vol.26 , Issue.18 , pp. 3911-3918
    • Chen, Y.-S.1    Chang, J.-Y.2    Cheng, C.-Y.3    Tsai, F.-J.4    Yao, C.-H.5    Liu, B.-S.6
  • 13
    • 27744470669 scopus 로고    scopus 로고
    • Effect of gelatin on the swelling behavior of organic hybrid gels based on N-isopropylacrylamide and gelatin
    • DOI 10.1002/app.21287
    • Lee, W.; Lee, S. Effect of gelatin on the swelling behavior of organic hybrid gels based on N -isopropylacrylamide and gelatin J. Appl. Polym. Sci. 2005, 98 (3) 1092-1099 (Pubitemid 41625187)
    • (2005) Journal of Applied Polymer Science , vol.98 , Issue.3 , pp. 1092-1099
    • Lee, W.-F.1    Lee, S.-C.2
  • 14
  • 15
    • 78751575291 scopus 로고    scopus 로고
    • Effects of different cross-linking conditions on the properties of genipin-cross-linked chitosan/collagen scaffolds for cartilage tissue engineering
    • Bi, L.; Cao, Z.; Hu, Y.; Song, Y.; Yu, L.; Yang, B.; Mu, J.; Huang, Z.; Han, Y. Effects of different cross-linking conditions on the properties of genipin-cross-linked chitosan/collagen scaffolds for cartilage tissue engineering J. Mater. Sci. Mater. Med. 2011, 22 (1) 51-62
    • (2011) J. Mater. Sci. Mater. Med. , vol.22 , Issue.1 , pp. 51-62
    • Bi, L.1    Cao, Z.2    Hu, Y.3    Song, Y.4    Yu, L.5    Yang, B.6    Mu, J.7    Huang, Z.8    Han, Y.9
  • 16
    • 78149412175 scopus 로고    scopus 로고
    • Naturally crosslinked gelatin gels with modified material properties
    • Kosaraju, S.; Puvanenthiran, A.; Lillford, P. Naturally crosslinked gelatin gels with modified material properties Food Res. Int. 2010, 43 (10) 2385-2389
    • (2010) Food Res. Int. , vol.43 , Issue.10 , pp. 2385-2389
    • Kosaraju, S.1    Puvanenthiran, A.2    Lillford, P.3
  • 17
    • 64749115024 scopus 로고    scopus 로고
    • Genipin-crosslinked chitosan hydrogels as biomedical and pharmaceutical aids
    • Muzzarelli, R. Genipin-crosslinked chitosan hydrogels as biomedical and pharmaceutical aids Carbohydr. Polym. 2009, 77 (1) 1-9
    • (2009) Carbohydr. Polym. , vol.77 , Issue.1 , pp. 1-9
    • Muzzarelli, R.1
  • 18
    • 0027932731 scopus 로고
    • Studies on the blue pigments produced from genipin and methylamine. II. On the formation mechanisms of brownish-red intermediates leading to the blue pigment formation
    • Touyama, R.; Inoue, K.; Takeda, Y.; Yatsuzuka, M.; Ikumoto, T.; Moritome, N.; Shingu, T.; Yokoi, T.; Inouye, H. Studies on the blue pigments produced from genipin and methylamine. II. On the formation mechanisms of brownish-red intermediates leading to the blue pigment formation Chem. Pharm. Bull. 1994, 42, 1571-1578 (Pubitemid 24276149)
    • (1994) Chemical and Pharmaceutical Bulletin , vol.42 , Issue.8 , pp. 1571-1578
    • Touyama, R.1    Inoue, K.2    Takeda, Y.3    Yatsuzuka, M.4    Ikumoto, T.5    Moritome, N.6    Shingu, T.7    Yokoi, T.8    Inouye, H.9
  • 19
    • 0037464373 scopus 로고    scopus 로고
    • Colorimetric determination of amino acids using genipin from Gardenia jasminoides
    • DOI 10.1016/S0003-2670(03)00023-0
    • Lee, S.; Lim, J.; Bhoo, S.; Paik, Y.; Hahn, T. Colorimetric determination of amino acids using genipin from Gardenia jasminoides Anal. Chim. Acta 2003, 480 (2) 267-274 (Pubitemid 36254844)
    • (2003) Analytica Chimica Acta , vol.480 , Issue.2 , pp. 267-274
    • Lee, S.-W.1    Lim, J.-M.2    Bhoo, S.-H.3    Paik, Y.-S.4    Hahn, T.-R.5
  • 20
    • 0000319609 scopus 로고    scopus 로고
    • Physicochemical Characteristics for the Transformation of Blue Pigments from Genipin of Gardenia jasminoides with Amino Acids
    • Lee, J.; Hahn, T.; Paik, Y. Physicochemical characteristics for the transformation of blue pigments from genipin of Gardenia jasminoides with amino acids Agric. Chem. Biotechnol. 1998, 41 (5) 399-404 (Pubitemid 128151803)
    • (1998) Agric. Chem. Biotechnol. , vol.41 , Issue.5 , pp. 399-404
    • Lee, J.-Y.1    Hahn, T.-R.2    Paik, Y.-S.3
  • 21
    • 17744370299 scopus 로고    scopus 로고
    • Physical stability of the blue pigments formed from geniposide of gardenia fruits: Effects of ph, temperature, and light
    • DOI 10.1021/jf000978f
    • Paik, Y.; Lee, C.; Cho, M.; Hahn, T. Physical stability of the blue pigments formed from geniposide of Gardenia fruits: Effects of pH, temperature, and light J. Agric. Food Chem. 2001, 49 (1) 430-432 (Pubitemid 32104545)
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , Issue.1 , pp. 430-432
    • Paik, Y.-S.1    Lee, C.-M.2    Cho, M.-H.3    Hahn, T.-R.4
  • 23
    • 0034684161 scopus 로고    scopus 로고
    • The core lipocalin, bovine β-lactoglobulin
    • Sawyer, L.; Kontopidis, G. The core lipocalin, bovine β-lactoglobulin Biochim. Biophys. Acta 2000, 1482 (1-2) 136-148
    • (2000) Biochim. Biophys. Acta , vol.1482 , Issue.1-2 , pp. 136-148
    • Sawyer, L.1    Kontopidis, G.2
  • 24
    • 0033810124 scopus 로고    scopus 로고
    • Conformation and stability of thiol-modified bovine β-lactoglobulin
    • Sakai, K.; Sakurai, K.; Sakai, M.; Hoshino, M.; Goto, Y. Conformation and stability of thiol-modified bovine β-lactoglobulin Protein Sci. 2000, 9 (9) 1719-1729
    • (2000) Protein Sci. , vol.9 , Issue.9 , pp. 1719-1729
    • Sakai, K.1    Sakurai, K.2    Sakai, M.3    Hoshino, M.4    Goto, Y.5
  • 25
    • 0000008542 scopus 로고    scopus 로고
    • Heat-Induced Aggregation of β-Lactoglobulin: Role of the Free Thiol Group and Disulfide Bonds
    • Hoffmann, M. A. M.; van Mil, P. J. J. M. Heat-induced aggregation of β-lactoglobulin: Role of the free thiol group and disulfide bonds J. Agric. Food Chem. 1997, 45 (8) 2942-2948 (Pubitemid 127481834)
    • (1997) Journal of Agricultural and Food Chemistry , vol.45 , Issue.8 , pp. 2942-2948
    • Hoffmann, M.A.M.1    Van Mil, P.J.J.M.2
  • 27
    • 0000512387 scopus 로고
    • The unfolding of β-lactoglobulin at pH 3 by urea, formamide, and other organic substances
    • Tanford, C.; De, P. K. The unfolding of β-lactoglobulin at pH 3 by urea, formamide, and other organic substances J. Biol. Chem. 1961, 236 (6) 1711-1715
    • (1961) J. Biol. Chem. , vol.236 , Issue.6 , pp. 1711-1715
    • Tanford, C.1    De, P.K.2
  • 28
    • 0000620595 scopus 로고
    • β-Lactoglobulins
    • Bell, K.; McKenzie, H. A. β-Lactoglobulins Nature 1964, 204 (4965) 1275-1279
    • (1964) Nature , vol.204 , Issue.4965 , pp. 1275-1279
    • Bell, K.1    McKenzie, H.A.2
  • 29
    • 0014010079 scopus 로고
    • Infrared investigation of the secondary structure of β- lactoglobulins
    • Timasheff, S. N.; Susi, H. Infrared investigation of the secondary structure of β-lactoglobulins J. Biol. Chem. 1966, 241 (1) 249-251
    • (1966) J. Biol. Chem. , vol.241 , Issue.1 , pp. 249-251
    • Timasheff, S.N.1    Susi, H.2
  • 30
    • 0001497241 scopus 로고
    • The reversible transformation of β-lactoglobulin at pH 7.51
    • Tanford, C.; Bunville, L. G.; Nozaki, Y. The reversible transformation of β-lactoglobulin at pH 7.51 J. Am. Chem. Soc. 1959, 81 (15) 4032-4036
    • (1959) J. Am. Chem. Soc. , vol.81 , Issue.15 , pp. 4032-4036
    • Tanford, C.1    Bunville, L.G.2    Nozaki, Y.3
  • 31
    • 0344012492 scopus 로고    scopus 로고
    • Reversible Unfolding of Bovine β-Lactoglobulin Mutants without a Free Thiol Group
    • DOI 10.1074/jbc.M308592200
    • Yagi, M.; Sakurai, K.; Kalidas, C.; Batt, C. A.; Goto, Y. Reversible unfolding of bovine β-lactoglobulin mutants without a free thiol group J. Biol. Chem. 2003, 278 (47) 47009-47015 (Pubitemid 37452284)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.47 , pp. 47009-47015
    • Yagi, M.1    Sakurai, K.2    Kalidas, C.3    Batt, C.A.4    Goto, Y.5
  • 32
    • 30744476205 scopus 로고    scopus 로고
    • Dynamics and mechanism of the tanford transition of bovine β-lactoglobulin studied using heteronuclear NMR spectroscopy
    • DOI 10.1016/j.jmb.2005.11.038, PII S0022283605014269
    • Sakurai, K.; Goto, Y. Dynamics and mechanism of the Tanford transition of bovine β-lactoglobulin studied using heteronuclear NMR spectroscopy J. Mol. Biol. 2006, 356 (2) 483-496 (Pubitemid 43099985)
    • (2006) Journal of Molecular Biology , vol.356 , Issue.2 , pp. 483-496
    • Sakurai, K.1    Goto, Y.2
  • 33
    • 0035824880 scopus 로고    scopus 로고
    • Characterization of pH-induced transitions of β-lactoglobulin: Ultrasonic, densimetric, and spectroscopic studies
    • DOI 10.1006/jmbi.2001.5188
    • Taulier, N.; Chalikian, T. V. Characterization of pH-induced transitions of β-lactoglobulin: Ultrasonic, densimetric, and spectroscopic studies J. Mol. Biol. 2001, 314 (4) 873-889 (Pubitemid 34087854)
    • (2001) Journal of Molecular Biology , vol.314 , Issue.4 , pp. 873-889
    • Taulier, N.1    Chalikian, T.V.2
  • 34
    • 44449152167 scopus 로고    scopus 로고
    • Disulfide-linked bovine β-lactoglobulin dimers fold slowly, navigating a glassy folding landscape
    • DOI 10.1021/bi8001715
    • Yagi, M.; Kameda, A.; Sakurai, K.; Nishimura, C.; Goto, Y. Disulfide-linked bovine β-lactoglobulin dimers fold slowly, navigating a glassy folding landscape Biochemistry 2008, 47 (22) 5996-6006 (Pubitemid 351770029)
    • (2008) Biochemistry , vol.47 , Issue.22 , pp. 5996-6006
    • Yagi, M.1    Kameda, A.2    Sakurai, K.3    Nishimura, C.4    Goto, Y.5
  • 35
    • 0000819131 scopus 로고
    • Molecular interactions in β-lactoglobulin. II. Ultracentrifugal and electrophoretic studies of the association of β-lactoglobulin below its isoelectric point
    • Townend, R.; Winterbottom, R. J.; Timasheff, S. N. Molecular interactions in β-lactoglobulin. II. Ultracentrifugal and electrophoretic studies of the association of β-lactoglobulin below its isoelectric point J. Am. Chem. Soc. 1960, 82 (12) 3161-3168
    • (1960) J. Am. Chem. Soc. , vol.82 , Issue.12 , pp. 3161-3168
    • Townend, R.1    Winterbottom, R.J.2    Timasheff, S.N.3
  • 36
    • 0000819132 scopus 로고
    • Molecular interactions in β-lactoglobulin. IV. The dissociation of β-lactoglobulin below pH 3.52
    • Townend, R.; Weinberger, L.; Timasheff, S. N. Molecular interactions in β-lactoglobulin. IV. The dissociation of β-lactoglobulin below pH 3.52 J. Am. Chem. Soc. 1960, 82 (12) 3175-3179
    • (1960) J. Am. Chem. Soc. , vol.82 , Issue.12 , pp. 3175-3179
    • Townend, R.1    Weinberger, L.2    Timasheff, S.N.3
  • 37
    • 0019331938 scopus 로고
    • A differential scanning calorimetric study of the thermal denaturation of bovine β-lactoglobulin. Thermal behaviour at temperatures up to 100 °C
    • de Wit, J. N.; Swinkels, G. A. A differential scanning calorimetric study of the thermal denaturation of bovine β-lactoglobulin. Thermal behaviour at temperatures up to 100 °C Biochim. Biophys. Acta 1980, 624 (1) 40-50
    • (1980) Biochim. Biophys. Acta , vol.624 , Issue.1 , pp. 40-50
    • De Wit, J.N.1    Swinkels, G.A.2
  • 38
    • 33744534909 scopus 로고    scopus 로고
    • Effects of heating at neutral and acid pH on the structure of β-lactoglobulin A revealed by differential scanning calorimetry and circular dichroism spectroscopy
    • DOI 10.1016/j.bbagen.2005.12.025, PII S030441650600002X
    • Wada, R.; Fujita, Y.; Kitabatake, N. Effects of heating at neutral and acid pH on the structure of β-lactoglobulin A revealed by differential scanning calorimetry and circular dichroism spectroscopy Biochim. Biophys. Acta 2006, 1760 (6) 841-847 (Pubitemid 43816173)
    • (2006) Biochimica et Biophysica Acta - General Subjects , vol.1760 , Issue.6 , pp. 841-847
    • Wada, R.1    Fujita, Y.2    Kitabatake, N.3
  • 39
    • 0030993642 scopus 로고    scopus 로고
    • Effect of temperature on the secondary structure of β-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: A test of the molten globule hypothesis
    • Qi, X. L.; Holt, C.; McNulty, D.; Clarke, D. T.; Brownlow, S.; Jones, G. R. Effect of temperature on the secondary structure of β-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: A test of the molten globule hypothesis Biochem. J. 1997, 324 (Part 3) 341-346 (Pubitemid 27229401)
    • (1997) Biochemical Journal , vol.324 , Issue.1 , pp. 341-346
    • Qi, X.L.1    Holt, C.2    Mcnulty, D.3    Clarke, D.T.4    Brownlow, S.5    Jones, G.R.6
  • 40
    • 0030272655 scopus 로고    scopus 로고
    • The effect of temperature and ionic strength on the dimerisation of β-lactoglobulin
    • DOI 10.1016/0141-8130(96)01130-0
    • Aymard, P.; Durand, D.; Nicolai, T. The effect of temperature and ionic strength on the dimerisation of β-lactoglobulin Int. J. Biol. Macromol. 1996, 19 (3) 213-221 (Pubitemid 26354240)
    • (1996) International Journal of Biological Macromolecules , vol.19 , Issue.3 , pp. 213-221
    • Aymard, P.1    Durand, D.2    Nicolai, T.3
  • 41
    • 79959908730 scopus 로고    scopus 로고
    • Loosening of globular structure under alkaline pH affects accessibility of β-lactoglobulin to tyrosinase-induced oxidation and subsequent cross-linking
    • Partanen, R.; Torkkeli, M.; Hellman, M.; Permi, P.; Serimaa, R.; Buchert, J.; Mattinen, M.-L. Loosening of globular structure under alkaline pH affects accessibility of β-lactoglobulin to tyrosinase-induced oxidation and subsequent cross-linking Enzyme Microb. Technol. 2011, 49 (2) 131-138
    • (2011) Enzyme Microb. Technol. , vol.49 , Issue.2 , pp. 131-138
    • Partanen, R.1    Torkkeli, M.2    Hellman, M.3    Permi, P.4    Serimaa, R.5    Buchert, J.6    Mattinen, M.-L.7
  • 42
    • 0026510654 scopus 로고
    • Transglutaminase catalyses the modification of glutamine side chains in the C-terminal region of bovine β-lactoglobulin
    • Coussons, P. J.; Price, N. C.; Kelly, S. M.; Smith, B.; Sawyer, L. Transglutaminase catalyses the modification of glutamine side chains in the C-terminal region of bovine β-lactoglobulin Biochem. J. 1992, 283 (Part 3) 803-806
    • (1992) Biochem. J. , vol.283 , Issue.PART 3 , pp. 803-806
    • Coussons, P.J.1    Price, N.C.2    Kelly, S.M.3    Smith, B.4    Sawyer, L.5
  • 43
    • 0842278662 scopus 로고    scopus 로고
    • Transglutaminase-Mediated Modification of Glutamine and Lysine Residues in Native Bovine β-Lactoglobulin
    • DOI 10.1002/bit.10898
    • Nieuwenhuizen, W. F.; Dekker, H. L.; Groneveld, T.; De Koster, C. G.; De Jong, G. A. Transglutaminase-mediated modification of glutamine and lysine residues in native bovine β-lactoglobulin Biotechnol. Bioeng. 2004, 85 (3) 248-258 (Pubitemid 38182217)
    • (2004) Biotechnology and Bioengineering , vol.85 , Issue.3 , pp. 248-258
    • Nieuwenhuizen, W.F.1    Dekker, H.L.2    Groneveld, T.3    De Koster, C.G.4    De Jong, G.A.H.5
  • 44
    • 79956318961 scopus 로고    scopus 로고
    • Comparison between structural changes of heat-treated and transglutaminase cross-linked β-lactoglobulin and their effects on foaming properties
    • Baez, G. D.; Moro, A.; Ballerinia, G. A.; Busti, P. A.; Delorenzi, N. J. Comparison between structural changes of heat-treated and transglutaminase cross-linked β-lactoglobulin and their effects on foaming properties Food Hydrocolloids 2011, 25 (7) 1758-1765
    • (2011) Food Hydrocolloids , vol.25 , Issue.7 , pp. 1758-1765
    • Baez, G.D.1    Moro, A.2    Ballerinia, G.A.3    Busti, P.A.4    Delorenzi, N.J.5
  • 45
    • 33745609556 scopus 로고    scopus 로고
    • Enzymatic cross-linking of β-lactoglobulin: Conformational properties using FTIR spectroscopy
    • DOI 10.1021/bm050928p
    • Eissa, A. S.; Puhl, C.; Kadla, J. F.; Khan, S. A. Enzymatic cross-linking of β-lactoglobulin: Conformational properties using FTIR spectroscopy Biomacromolecules 2006, 7 (6) 1707-1713 (Pubitemid 43985088)
    • (2006) Biomacromolecules , vol.7 , Issue.6 , pp. 1707-1713
    • Eissa, A.S.1    Puhl, C.2    Kadla, J.F.3    Khan, S.A.4
  • 47
    • 79955086146 scopus 로고    scopus 로고
    • Physical properties, molecular structures and protein quality of texturized whey protein isolate (WPI): Effect of extrusion temperature
    • Qi, P. X.; Onwulata, C. I. Physical properties, molecular structures and protein quality of texturized whey protein isolate (WPI): Effect of extrusion temperature J. Agric. Food Chem. 2011, 59 (9) 4668-4675
    • (2011) J. Agric. Food Chem. , vol.59 , Issue.9 , pp. 4668-4675
    • Qi, P.X.1    Onwulata, C.I.2
  • 49
    • 0037164092 scopus 로고    scopus 로고
    • Isolation and characterization of water-soluble intermediates of blue pigments transformed from geniposide of Gardenia jasminoides
    • DOI 10.1021/jf020499b
    • Park, J.; Lee, J.; Kim, H.; Hahn, T.; Paik, Y. Isolation and characterization of water-soluble intermediates of blue pigments transformed from geniposide of Gardenia jasminoides J. Agric. Food Chem. 2002, 50 (22) 6511-6514 (Pubitemid 35216763)
    • (2002) Journal of Agricultural and Food Chemistry , vol.50 , Issue.22 , pp. 6511-6514
    • Park, J.-E.1    Lee, J.-Y.2    Kim, H.-G.3    Hahn, T.-R.4    Paik, Y.-S.5
  • 50
    • 0035339420 scopus 로고    scopus 로고
    • A ninhydrin-based assay to quantitate the total protein content of tissue samples
    • DOI 10.1006/abio.2001.5050
    • Starcher, B. A ninhydrin-based assay to quantitate the total protein content of tissue samples Anal. Biochem. 2001, 292 (1) 125-129 (Pubitemid 32417730)
    • (2001) Analytical Biochemistry , vol.292 , Issue.1 , pp. 125-129
    • Starcher, B.1
  • 51
    • 84860479726 scopus 로고    scopus 로고
    • 2 nd ed. Elsevier, Ltd. Amsterdam, The Netherlands, Vol.
    • Helfferich, F. G. Kinetics of Multistep Reactions, 2 nd ed.; Elsevier, Ltd.: Amsterdam, The Netherlands, 2004; Vol. 40, p 488.
    • (2004) Kinetics of Multistep Reactions , vol.40 , pp. 488
    • Helfferich, F.G.1
  • 52
    • 19844366411 scopus 로고    scopus 로고
    • Characterization of ring-opening polymerization of genipin and pH-dependent cross-linking reactions between chitosan and genipin
    • DOI 10.1002/pola.20669
    • Mi, F.; Shyu, S.; Peng, C. Characterization of ring-opening polymerization of genipin and pH-dependent cross-linking reactions between chitosan and genipin J. Polym. Sci., Part A: Polym. Chem. 2005, 43 (10) 1985-2000 (Pubitemid 40760968)
    • (2005) Journal of Polymer Science, Part A: Polymer Chemistry , vol.43 , Issue.10 , pp. 1985-2000
    • Mi, F.-L.1    Shyu, S.-S.2    Peng, C.-K.3
  • 53
    • 78751520292 scopus 로고    scopus 로고
    • Kinetic analysis of genipin degradation in aqueous solution
    • Slusarewicz, P.; Zhu, K.; Hedman, T. Kinetic analysis of genipin degradation in aqueous solution Nat. Prod. Commun. 2010, 5 (12) 1853-1858
    • (2010) Nat. Prod. Commun. , vol.5 , Issue.12 , pp. 1853-1858
    • Slusarewicz, P.1    Zhu, K.2    Hedman, T.3
  • 54
    • 0023802035 scopus 로고
    • Accessibility and mobility of lysine residues in β-lactoglobulin
    • Brown, E. M.; Pfeffer, P. E.; Kumosinski, T. F.; Greenberg, R. Accessibility and mobility of lysine residues in β-lactoglobulin Biochemistry 1988, 27 (15) 5601-5610
    • (1988) Biochemistry , vol.27 , Issue.15 , pp. 5601-5610
    • Brown, E.M.1    Pfeffer, P.E.2    Kumosinski, T.F.3    Greenberg, R.4
  • 55
    • 85010630698 scopus 로고
    • Differential scanning calorimetric study of different genetic variants of β-lactoglobulin
    • Imafidon, G. I.; Ng-Kwai-Hang, K. F.; Harwalkar, V. R.; Ma, C. Y. Differential scanning calorimetric study of different genetic variants of β-lactoglobulin J. Dairy Sci. 1991, 74 (8) 2416-2422
    • (1991) J. Dairy Sci. , vol.74 , Issue.8 , pp. 2416-2422
    • Imafidon, G.I.1    Ng-Kwai-Hang, K.F.2    Harwalkar, V.R.3    Ma, C.Y.4


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