메뉴 건너뛰기




Volumn 188, Issue , 2015, Pages 8-14

Sweetness characterization of recombinant human lysozyme

Author keywords

Human lysozyme; Milk; Pichia pastoris; Sweet taste receptor; Sweetness

Indexed keywords

AMINO ACID; LYSOZYME; RECOMBINANT ENZYME; RECOMBINANT PROTEIN;

EID: 84930934307     PISSN: 10964959     EISSN: 18791107     Source Type: Journal    
DOI: 10.1016/j.cbpb.2015.05.009     Document Type: Article
Times cited : (4)

References (40)
  • 3
    • 14644415512 scopus 로고    scopus 로고
    • Expression of sweet taste receptors of the T1R family in the intestinal tract and enteroendocrine cells
    • Dyer J., Salmon K.S.H., Zibrik L., Shirazi-Beechey S.P. Expression of sweet taste receptors of the T1R family in the intestinal tract and enteroendocrine cells. Biochem. Soc. Trans. 2005, 33:302-305.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 302-305
    • Dyer, J.1    Salmon, K.S.H.2    Zibrik, L.3    Shirazi-Beechey, S.P.4
  • 4
    • 33745253400 scopus 로고    scopus 로고
    • The importance of electrostatic potential in the interaction of sweet proteins with the sweet taste receptor
    • Esposito V., Gallucci R., Picone D., Saviano G., Tancredi T., Temussi P.A. The importance of electrostatic potential in the interaction of sweet proteins with the sweet taste receptor. J. Mol. Biol. 2006, 360:448-456.
    • (2006) J. Mol. Biol. , vol.360 , pp. 448-456
    • Esposito, V.1    Gallucci, R.2    Picone, D.3    Saviano, G.4    Tancredi, T.5    Temussi, P.A.6
  • 5
    • 0000461280 scopus 로고
    • Confidence limits on phylogenies: an approach using the bootstrap
    • Felsenstein J. Confidence limits on phylogenies: an approach using the bootstrap. Evolution 1985, 39:783-791.
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 7
    • 0035941271 scopus 로고    scopus 로고
    • A helix-loop-helix peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action
    • Ibrahim H.R., Thomas U., Pellegrini A. A helix-loop-helix peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action. J. Biol. Chem. 2001, 276:43767-43774.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43767-43774
    • Ibrahim, H.R.1    Thomas, U.2    Pellegrini, A.3
  • 8
    • 67649875867 scopus 로고    scopus 로고
    • Interactions of the sweet-tasting proteins thaumatin and lysozyme with the human sweet-taste receptor
    • Ide N., Sato E., Ohta K., Masuda T., Kitabatake N. Interactions of the sweet-tasting proteins thaumatin and lysozyme with the human sweet-taste receptor. J. Agric. Food Chem. 2009, 57:5884-5890.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 5884-5890
    • Ide, N.1    Sato, E.2    Ohta, K.3    Masuda, T.4    Kitabatake, N.5
  • 10
    • 19544381690 scopus 로고
    • A simple activity measurement of lysozyme
    • Imoto T., Yagishita K. A simple activity measurement of lysozyme. Agric. Biol. Chem. 1971, 35:1154-1156.
    • (1971) Agric. Biol. Chem. , vol.35 , pp. 1154-1156
    • Imoto, T.1    Yagishita, K.2
  • 11
    • 15444373235 scopus 로고    scopus 로고
    • Evolution of cow nonstomach lysozyme genes
    • Irwin D.M. Evolution of cow nonstomach lysozyme genes. Genome 2004, 47:1082-1090.
    • (2004) Genome , vol.47 , pp. 1082-1090
    • Irwin, D.M.1
  • 13
    • 15744376671 scopus 로고    scopus 로고
    • Sweet proteins-potential replacement for artificial low calorie sweeteners
    • Kant R. Sweet proteins-potential replacement for artificial low calorie sweeteners. Nutr. J. 2005, 4:1-5.
    • (2005) Nutr. J. , vol.4 , pp. 1-5
    • Kant, R.1
  • 14
    • 0024402332 scopus 로고
    • Enhanced bacteriolytic activity of hen egg-white lysozyme due to conversion of Trp62 to other aromatic amino acid residues
    • Kumagai I., Miura K. Enhanced bacteriolytic activity of hen egg-white lysozyme due to conversion of Trp62 to other aromatic amino acid residues. J. Biochem. 1989, 105:946-948.
    • (1989) J. Biochem. , vol.105 , pp. 946-948
    • Kumagai, I.1    Miura, K.2
  • 15
    • 0027530690 scopus 로고
    • Effects of subsite alterations on substrate-binding mode in the active site of hen egg-white lysozyme
    • Kumagai I., Maenaka K., Sunada F., Takeda S., Miura K. Effects of subsite alterations on substrate-binding mode in the active site of hen egg-white lysozyme. Eur. J. Biochem. 1993, 212:151-156.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 151-156
    • Kumagai, I.1    Maenaka, K.2    Sunada, F.3    Takeda, S.4    Miura, K.5
  • 16
    • 0022497306 scopus 로고
    • Specific carbodiimide-binding mechanism for the selective modification of the aspartic acid-101 residue of lysozyme in the carbodiimide-amine reaction
    • Kuroki R., Yamada H., Imoto T. Specific carbodiimide-binding mechanism for the selective modification of the aspartic acid-101 residue of lysozyme in the carbodiimide-amine reaction. J. Biochem. 1986, 99:1493-1499.
    • (1986) J. Biochem. , vol.99 , pp. 1493-1499
    • Kuroki, R.1    Yamada, H.2    Imoto, T.3
  • 17
    • 0019842272 scopus 로고
    • Lysozyme enhances monocyte-mediated tumoricidal activity: a potential amplifying mechanism of tumor killing
    • Le Marbre P., Rinehart J.J., Kay N.E., Vesella R., Jacob H.S. Lysozyme enhances monocyte-mediated tumoricidal activity: a potential amplifying mechanism of tumor killing. Blood 1981, 58:994-999.
    • (1981) Blood , vol.58 , pp. 994-999
    • Le Marbre, P.1    Rinehart, J.J.2    Kay, N.E.3    Vesella, R.4    Jacob, H.S.5
  • 22
    • 84155195135 scopus 로고    scopus 로고
    • Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white
    • Maehashi K., Matano M., Irisawa T., Uchino M., Kashiwagi Y., Watanabe T. Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white. Gene 2012, 492:244-249.
    • (2012) Gene , vol.492 , pp. 244-249
    • Maehashi, K.1    Matano, M.2    Irisawa, T.3    Uchino, M.4    Kashiwagi, Y.5    Watanabe, T.6
  • 23
    • 33747063054 scopus 로고    scopus 로고
    • Consumption of milk from transgenic goats expressing human lysozyme in the mammary gland results in the modulation of intestinal microflara
    • Maga E.A., Walker R.L., Anderson G.B., Murray J.D. Consumption of milk from transgenic goats expressing human lysozyme in the mammary gland results in the modulation of intestinal microflara. Transgenic Res. 2006, 15:515-519.
    • (2006) Transgenic Res. , vol.15 , pp. 515-519
    • Maga, E.A.1    Walker, R.L.2    Anderson, G.B.3    Murray, J.D.4
  • 26
    • 0034769595 scopus 로고    scopus 로고
    • Sweetness and enzymatic activity of lysozyme
    • Masuda T., Ueno Y., Kitabatake N. Sweetness and enzymatic activity of lysozyme. J. Agric. Food Chem. 2001, 49:4937-4941.
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 4937-4941
    • Masuda, T.1    Ueno, Y.2    Kitabatake, N.3
  • 27
    • 27244449766 scopus 로고    scopus 로고
    • Structure-sweetness relationship in egg white lysozyme: role of lysine and arginine residues on the elicitation of lysozyme sweetness
    • Masuda T., Ide N., Kitabatake N. Structure-sweetness relationship in egg white lysozyme: role of lysine and arginine residues on the elicitation of lysozyme sweetness. Chem. Senses 2005, 30:667-681.
    • (2005) Chem. Senses , vol.30 , pp. 667-681
    • Masuda, T.1    Ide, N.2    Kitabatake, N.3
  • 28
    • 0038175138 scopus 로고    scopus 로고
    • A molecular basis for the endo-β1,3-glucanase activity of the thaumatin-like proteins from edible fruits
    • Menu-Bouaouiche L., Vriet C., Peumans W.J., Barre A., Van Damme E.J.M., Rougé P. A molecular basis for the endo-β1,3-glucanase activity of the thaumatin-like proteins from edible fruits. Biochimie 2003, 85:123-131.
    • (2003) Biochimie , vol.85 , pp. 123-131
    • Menu-Bouaouiche, L.1    Vriet, C.2    Peumans, W.J.3    Barre, A.4    Van Damme, E.J.M.5    Rougé, P.6
  • 29
    • 0032991055 scopus 로고    scopus 로고
    • 15N-labeled henlysozyme in Pichia pastoris and identification of the site in hen lysozyme where phosphate ion bind using NMR measurements
    • 15N-labeled henlysozyme in Pichia pastoris and identification of the site in hen lysozyme where phosphate ion bind using NMR measurements. FEBS Lett. 1999, 448:33-37.
    • (1999) FEBS Lett. , vol.448 , pp. 33-37
    • Mine, S.1    Ueda, T.2    Hashimoto, Y.3    Tanaka, Y.4    Imoto, T.5
  • 30
    • 23944498549 scopus 로고    scopus 로고
    • From small sweeteners to sweet proteins: anatomy of the binding sites of the human T1R2_T1R3 receptor
    • Morini G., Bassoli A., Temussi P.A. From small sweeteners to sweet proteins: anatomy of the binding sites of the human T1R2_T1R3 receptor. J. Med. Chem. 2005, 48:5520-5529.
    • (2005) J. Med. Chem. , vol.48 , pp. 5520-5529
    • Morini, G.1    Bassoli, A.2    Temussi, P.A.3
  • 31
    • 0023640447 scopus 로고
    • The roles of conserved aromatic amino-acid residues in the active site of human lysozyme: a site-specific mutagenesis study
    • Muraki M., Morikawa M., Jigami Y., Tanaka H. The roles of conserved aromatic amino-acid residues in the active site of human lysozyme: a site-specific mutagenesis study. Biochim. Biophys. Acta 1987, 916:66-75.
    • (1987) Biochim. Biophys. Acta , vol.916 , pp. 66-75
    • Muraki, M.1    Morikawa, M.2    Jigami, Y.3    Tanaka, H.4
  • 32
    • 0026806192 scopus 로고
    • Dissection of the functional role of structural elements of tyrosine-63 in the catalytic action of human lysozyme
    • Muraki M., Harata K., Jigami Y. Dissection of the functional role of structural elements of tyrosine-63 in the catalytic action of human lysozyme. Biochemistry 1992, 31:9212-9219.
    • (1992) Biochemistry , vol.31 , pp. 9212-9219
    • Muraki, M.1    Harata, K.2    Jigami, Y.3
  • 33
    • 0031042763 scopus 로고    scopus 로고
    • Importance of van der Waals contact between Glu 35 and Trp 109 to the catalytic action of human lysozyme
    • Muraki M., Goda S., Nagahora H., Harata K. Importance of van der Waals contact between Glu 35 and Trp 109 to the catalytic action of human lysozyme. Protein Sci. 1997, 6:473-476.
    • (1997) Protein Sci. , vol.6 , pp. 473-476
    • Muraki, M.1    Goda, S.2    Nagahora, H.3    Harata, K.4
  • 34
    • 0027162768 scopus 로고
    • Sweet-tasting protein monellin is related to the cystatin family of thiol proteinase inhibitors
    • Murzin A.G. Sweet-tasting protein monellin is related to the cystatin family of thiol proteinase inhibitors. J. Mol. Biol. 1993, 230:689-694.
    • (1993) J. Mol. Biol. , vol.230 , pp. 689-694
    • Murzin, A.G.1
  • 36
    • 0031774839 scopus 로고    scopus 로고
    • A novel anti-inflammatory activity of lysozyme: modulation of serum complement activation
    • Ogundele M.O. A novel anti-inflammatory activity of lysozyme: modulation of serum complement activation. Mediat. Inflamm. 1998, 7:363-365.
    • (1998) Mediat. Inflamm. , vol.7 , pp. 363-365
    • Ogundele, M.O.1
  • 38
    • 36949089946 scopus 로고
    • Disk electrophoresis of basic proteins and peptides on polyacrylamide gels
    • Reisfeld R.A., Lewis U.J., Williams D.E. Disk electrophoresis of basic proteins and peptides on polyacrylamide gels. Nature 1962, 195:281-283.
    • (1962) Nature , vol.195 , pp. 281-283
    • Reisfeld, R.A.1    Lewis, U.J.2    Williams, D.E.3
  • 39
    • 84875265866 scopus 로고    scopus 로고
    • The avian taste system: potential implications in poultry nutrition
    • Roura E., Baldwin M.W., Klasing K.C. The avian taste system: potential implications in poultry nutrition. Anim. Feed Sci. Technol. 2013, 180:1-9.
    • (2013) Anim. Feed Sci. Technol. , vol.180 , pp. 1-9
    • Roura, E.1    Baldwin, M.W.2    Klasing, K.C.3
  • 40
    • 0042739015 scopus 로고    scopus 로고
    • Functional interaction between T2R taste receptors and G-protein α subunits expressed in taste receptor cells
    • Ueda T., Ugawa S., Yamamura H., Imaizumi Y., Shimada S. Functional interaction between T2R taste receptors and G-protein α subunits expressed in taste receptor cells. J. Neurosci. 2003, 23:7376-7380.
    • (2003) J. Neurosci. , vol.23 , pp. 7376-7380
    • Ueda, T.1    Ugawa, S.2    Yamamura, H.3    Imaizumi, Y.4    Shimada, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.