메뉴 건너뛰기




Volumn 43, Issue 3, 2010, Pages 848-855

Multifunctional peptides from egg white lysozyme

Author keywords

Alcalase; Antioxidant activity; Calmodulin dependent phosphodiesterase; Hen's egg white lysozyme; Peptides

Indexed keywords

ALCALASE; ANTIOXIDANT ACTIVITIES; EGG WHITE; HEN'S EGG WHITE LYSOZYME; PHOSPHODIESTERASES;

EID: 76349107121     PISSN: 09639969     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodres.2009.12.004     Document Type: Article
Times cited : (141)

References (41)
  • 1
    • 33746299724 scopus 로고    scopus 로고
    • Antimicrobial peptides derived from hen egg lysozyme with inhibitory effect against Bacillus species
    • Abdou A.M., Higashiguchi S., Aboueleinin A.M., Kim M., and Ibrahim H.R. Antimicrobial peptides derived from hen egg lysozyme with inhibitory effect against Bacillus species. Food Control 18 (2007) 173-178
    • (2007) Food Control , vol.18 , pp. 173-178
    • Abdou, A.M.1    Higashiguchi, S.2    Aboueleinin, A.M.3    Kim, M.4    Ibrahim, H.R.5
  • 2
    • 0034852669 scopus 로고    scopus 로고
    • Effect of proline on the production of singlet oxygen
    • Alia M.P., and Matysick J. Effect of proline on the production of singlet oxygen. Amino Acids 21 (2001) 195-200
    • (2001) Amino Acids , vol.21 , pp. 195-200
    • Alia, M.P.1    Matysick, J.2
  • 3
    • 0031999603 scopus 로고    scopus 로고
    • Antioxidants from a heated histidine-glucose model system I. Investigation of the antioxidant role of histidine and isolation of antioxidants by high-performance liquid chromatography
    • Bersuder P., Hole M., and Smith G. Antioxidants from a heated histidine-glucose model system I. Investigation of the antioxidant role of histidine and isolation of antioxidants by high-performance liquid chromatography. Journal of the American Oil Chemists' Society 75 (1998) 181-187
    • (1998) Journal of the American Oil Chemists' Society , vol.75 , pp. 181-187
    • Bersuder, P.1    Hole, M.2    Smith, G.3
  • 5
    • 0002384554 scopus 로고    scopus 로고
    • Antioxidative properties of histidine-containing peptides designed from peptide fragments found in the digests of a soybean protein
    • Chen H.M., Muramoto K., Yamauchi F., Fujimoto K., and Nokihara K. Antioxidative properties of histidine-containing peptides designed from peptide fragments found in the digests of a soybean protein. Journal of Agricultural and Food Chemistry 46 (1998) 49-53
    • (1998) Journal of Agricultural and Food Chemistry , vol.46 , pp. 49-53
    • Chen, H.M.1    Muramoto, K.2    Yamauchi, F.3    Fujimoto, K.4    Nokihara, K.5
  • 7
    • 4444238114 scopus 로고    scopus 로고
    • Antioxidant activity of peptides derived from egg white proteins by enzymatic hydrolysis
    • Dávalos A., Miguel M., Bartolomé B., and López-Fandiňo R. Antioxidant activity of peptides derived from egg white proteins by enzymatic hydrolysis. Journal of Food Protection 67 9 (2004) 1939-1944
    • (2004) Journal of Food Protection , vol.67 , Issue.9 , pp. 1939-1944
    • Dávalos, A.1    Miguel, M.2    Bartolomé, B.3    López-Fandiňo, R.4
  • 8
    • 12844278044 scopus 로고    scopus 로고
    • The oxidative environment and protein damage
    • Davies M.J. The oxidative environment and protein damage. Biochimica et Biophysica Acta 1703 (2005) 93-109
    • (2005) Biochimica et Biophysica Acta , vol.1703 , pp. 93-109
    • Davies, M.J.1
  • 9
    • 0000130569 scopus 로고
    • Multiple range and multiple F test
    • Duncan D.B. Multiple range and multiple F test. Biometrics 11 (1955) 1-42
    • (1955) Biometrics , vol.11 , pp. 1-42
    • Duncan, D.B.1
  • 11
    • 51049097278 scopus 로고    scopus 로고
    • The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease
    • Erdmann K., Cheung B.W.Y., and Schroder H. The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease. The Journal of Nutritional Biochemistry 19 10 (2008) 634-654
    • (2008) The Journal of Nutritional Biochemistry , vol.19 , Issue.10 , pp. 634-654
    • Erdmann, K.1    Cheung, B.W.Y.2    Schroder, H.3
  • 12
    • 0024589610 scopus 로고
    • Antibacterial activity of hen white lysozyme against Listeria monocytogens Scott A in foods
    • Hughey V.L., Wilger P.A., and Johnson E.A. Antibacterial activity of hen white lysozyme against Listeria monocytogens Scott A in foods. Applied and Environmental Microbiology 55 3 (1989) 631-638
    • (1989) Applied and Environmental Microbiology , vol.55 , Issue.3 , pp. 631-638
    • Hughey, V.L.1    Wilger, P.A.2    Johnson, E.A.3
  • 13
    • 0001256923 scopus 로고    scopus 로고
    • Partially unfolded lysozyme at neutral pH agglutinates and kills Gram-negative and Gram-positive bacteria through membrane damage mechanism
    • Ibrahim H.R., Higashiguchi S., Koketsu M., Juneja L.R., Kim M., Yamamoto T., et al. Partially unfolded lysozyme at neutral pH agglutinates and kills Gram-negative and Gram-positive bacteria through membrane damage mechanism. Journal of Agricultural and Food Chemistry 44 12 (1996) 3799-3806
    • (1996) Journal of Agricultural and Food Chemistry , vol.44 , Issue.12 , pp. 3799-3806
    • Ibrahim, H.R.1    Higashiguchi, S.2    Koketsu, M.3    Juneja, L.R.4    Kim, M.5    Yamamoto, T.6
  • 14
    • 0035941271 scopus 로고    scopus 로고
    • A helix-loop 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., and Pellegrini A. A helix-loop peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action. The Journal of Biological Chemistry 276 47 (2001) 43767-43774
    • (2001) The Journal of Biological Chemistry , vol.276 , Issue.47 , pp. 43767-43774
    • Ibrahim, H.R.1    Thomas, U.2    Pellegrini, A.3
  • 15
    • 0019065883 scopus 로고
    • Interactions of basic polypeptides and proteins with calmodulin
    • Itano T., Itano R., and Penniston J.T. Interactions of basic polypeptides and proteins with calmodulin. The Biochemical Journal 189 (1980) 455-459
    • (1980) The Biochemical Journal , vol.189 , pp. 455-459
    • Itano, T.1    Itano, R.2    Penniston, J.T.3
  • 19
    • 33747503962 scopus 로고    scopus 로고
    • Bioactive peptide: Production and functionality
    • Korhonen H., and Pihlanto A. Bioactive peptide: Production and functionality. International Dairy Journal 16 (2006) 945-960
    • (2006) International Dairy Journal , vol.16 , pp. 945-960
    • Korhonen, H.1    Pihlanto, A.2
  • 20
    • 0031967750 scopus 로고    scopus 로고
    • Novel protein inhibitor of calmodulin-dependent cyclic nucleotide phosphodiesterase from glioblastoma multiforme
    • Lal S., Raju V.S., and Sharma K. Novel protein inhibitor of calmodulin-dependent cyclic nucleotide phosphodiesterase from glioblastoma multiforme. Neurochemical Research 23 4 (1998) 533-538
    • (1998) Neurochemical Research , vol.23 , Issue.4 , pp. 533-538
    • Lal, S.1    Raju, V.S.2    Sharma, K.3
  • 21
    • 26844440677 scopus 로고    scopus 로고
    • Kinetics of the inhibition of calcium/calmodulin-dependent protein kinase II by pea protein-derived peptides
    • Li H., and Aluko R.E. Kinetics of the inhibition of calcium/calmodulin-dependent protein kinase II by pea protein-derived peptides. The Journal of Nutritional Biochemistry 16 (2005) 656-662
    • (2005) The Journal of Nutritional Biochemistry , vol.16 , pp. 656-662
    • Li, H.1    Aluko, R.E.2
  • 23
    • 1542347593 scopus 로고    scopus 로고
    • Antimicrobial peptides released by enzymatic hydrolysis of hen egg white lysozyme
    • Mine Y., Ma F., and Lauriau S. Antimicrobial peptides released by enzymatic hydrolysis of hen egg white lysozyme. Journal of Agricultural and Food Chemistry 52 (2004) 1088-1094
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , pp. 1088-1094
    • Mine, Y.1    Ma, F.2    Lauriau, S.3
  • 24
    • 0036153931 scopus 로고    scopus 로고
    • Secretory peptide hormones are biochemical antioxidants: Structure-activity relationship
    • Moosmann B., and Behl C. Secretory peptide hormones are biochemical antioxidants: Structure-activity relationship. Molecular Pharmacology 61 (2002) 260-268
    • (2002) Molecular Pharmacology , vol.61 , pp. 260-268
    • Moosmann, B.1    Behl, C.2
  • 25
    • 33750350429 scopus 로고    scopus 로고
    • Effect of cationic flaxseed protein hydrolysate fractions on the in vitro structure and activity of calmodulin-dependent endothelial nitric oxide synthase
    • Omoni A., and Aluko R.E. Effect of cationic flaxseed protein hydrolysate fractions on the in vitro structure and activity of calmodulin-dependent endothelial nitric oxide synthase. Molecular Nutrition & Food Research 50 (2006) 958-966
    • (2006) Molecular Nutrition & Food Research , vol.50 , pp. 958-966
    • Omoni, A.1    Aluko, R.E.2
  • 26
    • 33847068206 scopus 로고    scopus 로고
    • Overview of PDEs and their regulation
    • Omori K., and Kotera J. Overview of PDEs and their regulation. Circulation Research 100 (2007) 309-327
    • (2007) Circulation Research , vol.100 , pp. 309-327
    • Omori, K.1    Kotera, J.2
  • 27
    • 0034773950 scopus 로고    scopus 로고
    • Development and validation of an improved oxygen radical absorbance capacity assay using fluorescein as the fluorescent probe
    • Ou B., Hampsch-Woodill M., and Prior R. Development and validation of an improved oxygen radical absorbance capacity assay using fluorescein as the fluorescent probe. Journal of Agricultural and Food Chemistry 49 (2001) 4619-4626
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , pp. 4619-4626
    • Ou, B.1    Hampsch-Woodill, M.2    Prior, R.3
  • 29
    • 0036813306 scopus 로고    scopus 로고
    • Antioxidative activity of soy protein hydrolysates in a liposomal system
    • Pena-Ramos E.A., and Xiong Y.L. Antioxidative activity of soy protein hydrolysates in a liposomal system. Journal of Food Science 67 (2002) 2952-2956
    • (2002) Journal of Food Science , vol.67 , pp. 2952-2956
    • Pena-Ramos, E.A.1    Xiong, Y.L.2
  • 31
    • 0023728756 scopus 로고
    • The chemistry of lysozyme and its use as a food preservative and as pharmaceutical
    • Proctor V.A., and Cunningham F.E. The chemistry of lysozyme and its use as a food preservative and as pharmaceutical. Critical Reviews in Food Science and Nutrition 26 (1988) 359-395
    • (1988) Critical Reviews in Food Science and Nutrition , vol.26 , pp. 359-395
    • Proctor, V.A.1    Cunningham, F.E.2
  • 34
    • 0030798636 scopus 로고    scopus 로고
    • Pitfalls in a method for assessment of total antioxidant capacity
    • Strube M., Haenen G.R.M.M., Berg H.V.D., and Bast A. Pitfalls in a method for assessment of total antioxidant capacity. Free Radical Research 26 (1997) 515-521
    • (1997) Free Radical Research , vol.26 , pp. 515-521
    • Strube, M.1    Haenen, G.R.M.M.2    Berg, H.V.D.3    Bast, A.4
  • 35
    • 0036120646 scopus 로고    scopus 로고
    • Clinical applications of antimicrobial host proteins lactoperoxidase, lysozyme and lactoferrin in xerostomia: Efficacy and safety
    • Tenuovo J. Clinical applications of antimicrobial host proteins lactoperoxidase, lysozyme and lactoferrin in xerostomia: Efficacy and safety. Oral Diseases 8 1 (2002) 23-29
    • (2002) Oral Diseases , vol.8 , Issue.1 , pp. 23-29
    • Tenuovo, J.1
  • 36
    • 4444329422 scopus 로고    scopus 로고
    • Reactive oxygen species, vascular oxidative stress and redox signaling in hypertension: What is the clinical significance?
    • Touyz R.M. Reactive oxygen species, vascular oxidative stress and redox signaling in hypertension: What is the clinical significance?. Hypertension 44 (2004) 248-252
    • (2004) Hypertension , vol.44 , pp. 248-252
    • Touyz, R.M.1
  • 37
    • 28444440308 scopus 로고    scopus 로고
    • Inhibition of lipid oxidation in cooked beef patties by hydrolyzed potato protein is related to its reducing and radical scavenging ability
    • Wang L.L., and Xiong Y.L. Inhibition of lipid oxidation in cooked beef patties by hydrolyzed potato protein is related to its reducing and radical scavenging ability. Journal of Agricultural and Food Chemistry 53 23 (2005) 9186-9192
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , Issue.23 , pp. 9186-9192
    • Wang, L.L.1    Xiong, Y.L.2
  • 38
    • 0015254094 scopus 로고
    • Rapid microassay of adenosine 3,5-monophosphate phosphodiesterase activity
    • Weiss B., Lehne R., and Strada S. Rapid microassay of adenosine 3,5-monophosphate phosphodiesterase activity. Analytical Biochemistry 45 (1972) 222-235
    • (1972) Analytical Biochemistry , vol.45 , pp. 222-235
    • Weiss, B.1    Lehne, R.2    Strada, S.3
  • 39
    • 0019947482 scopus 로고
    • Interaction of drugs with calmodulin: Biochemical, pharmacological and clinical implications
    • Weiss B., Prozialeck W.C., and Wallace T.L. Interaction of drugs with calmodulin: Biochemical, pharmacological and clinical implications. Biochemical Pharmacology 31 13 (1982) 2217-2226
    • (1982) Biochemical Pharmacology , vol.31 , Issue.13 , pp. 2217-2226
    • Weiss, B.1    Prozialeck, W.C.2    Wallace, T.L.3
  • 40
    • 10744230552 scopus 로고    scopus 로고
    • Free amino acids and peptides as related to antioxidant properties in protein hydrolysates of mackerel (Scomber austriasicus)
    • Wu H.C., Chen H.M., and Shiau C.Y. Free amino acids and peptides as related to antioxidant properties in protein hydrolysates of mackerel (Scomber austriasicus). Food Research International 36 (2003) 949-957
    • (2003) Food Research International , vol.36 , pp. 949-957
    • Wu, H.C.1    Chen, H.M.2    Shiau, C.Y.3
  • 41
    • 43649092437 scopus 로고    scopus 로고
    • Reducing, radical scavenging, and chelation properties of in vitro digests of Alcalase-treated zein hydrolysate
    • Zhu L., Chen C., Tang X., and Xiong Y. Reducing, radical scavenging, and chelation properties of in vitro digests of Alcalase-treated zein hydrolysate. Journal of Agricultural and Food Chemistry 56 (2008) 2714-2721
    • (2008) Journal of Agricultural and Food Chemistry , vol.56 , pp. 2714-2721
    • Zhu, L.1    Chen, C.2    Tang, X.3    Xiong, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.