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Volumn 100, Issue , 2017, Pages 121-133

Novel bioactive peptides from enzymatic hydrolysate of Sardinelle (Sardinella aurita) muscle proteins hydrolysed by Bacillus subtilis A26 proteases

Author keywords

Anti ACE; Antibacterial; Antioxidant; Peptide; Protein hydrolysate; Sardinella aurita

Indexed keywords

ANTIOXIDANTS; BACTERIOLOGY; CHROMATOGRAPHY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROLYSIS; ION EXCHANGE; LIQUID CHROMATOGRAPHY; ORGANIC POLYMERS; PEPTIDES; SIZE EXCLUSION CHROMATOGRAPHY;

EID: 85021833231     PISSN: 09639969     EISSN: 18737145     Source Type: Journal    
DOI: 10.1016/j.foodres.2017.06.018     Document Type: Article
Times cited : (54)

References (70)
  • 1
    • 84969641246 scopus 로고    scopus 로고
    • Combined biocatalytic conversion of smooth hound viscera: Protein hydrolysates elaboration and assessment of their antioxidant, anti-ACE and antibacterial activities
    • Abdelhedi, O., Jridi, M., Jemil, I., Mora, L., Toldrá, F., Aristoy, M.C. et al., Combined biocatalytic conversion of smooth hound viscera: Protein hydrolysates elaboration and assessment of their antioxidant, anti-ACE and antibacterial activities. Food Research International 86 (2016), 9–23.
    • (2016) Food Research International , vol.86 , pp. 9-23
    • Abdelhedi, O.1    Jridi, M.2    Jemil, I.3    Mora, L.4    Toldrá, F.5    Aristoy, M.C.6
  • 3
    • 0002494352 scopus 로고
    • A review of food hydrolysis specific areas
    • J. Adler-Nissen Elsevier Applied Science Publishers Copenhagen, Denmark
    • Adler-Nissen, J., A review of food hydrolysis specific areas. Adler-Nissen, J., (eds.) Enzymic hydrolysis of food proteins, 1986, Elsevier Applied Science Publishers, Copenhagen, Denmark, 57–109.
    • (1986) Enzymic hydrolysis of food proteins , pp. 57-109
    • Adler-Nissen, J.1
  • 4
    • 70349761446 scopus 로고    scopus 로고
    • Fibrinolytic enzymes from a newly isolated marine bacterium Bacillus subtilis A26: Characterization and statistical media optimization
    • Agrebi, R., Haddar, A., Hajji, M., Frikha, F., Manni, L., Jellouli, K. et al., Fibrinolytic enzymes from a newly isolated marine bacterium Bacillus subtilis A26: Characterization and statistical media optimization. Canadian Journal of Microbiology 55 (2009), 1049–1061.
    • (2009) Canadian Journal of Microbiology , vol.55 , pp. 1049-1061
    • Agrebi, R.1    Haddar, A.2    Hajji, M.3    Frikha, F.4    Manni, L.5    Jellouli, K.6
  • 6
    • 84870767152 scopus 로고    scopus 로고
    • Official methods of analysis
    • 17th edn Association of Official Analytical Chemists Washington
    • AOAC, Official methods of analysis. 17th edn, 2000, Association of Official Analytical Chemists, Washington.
    • (2000)
    • AOAC1
  • 7
    • 25044472884 scopus 로고
    • Deproteinization techniques for HPLC amino acid analyses in fresh pork muscle and dry cured ham
    • Aristoy, M.C., Toldrá, F., Deproteinization techniques for HPLC amino acid analyses in fresh pork muscle and dry cured ham. Journal of Agricultural and Food Chemistry 39 (1991), 1792–1795.
    • (1991) Journal of Agricultural and Food Chemistry , vol.39 , pp. 1792-1795
    • Aristoy, M.C.1    Toldrá, F.2
  • 8
    • 0020441144 scopus 로고
    • Rat intestinal brush border membrane dipeptidyl-aminopeptidase IV: Kinetic properties and substrate specifities of the purified enzyme
    • Bella, A.M. Jr., Erickson, R.H., Kim, Y.S., Rat intestinal brush border membrane dipeptidyl-aminopeptidase IV: Kinetic properties and substrate specifities of the purified enzyme. Archives of Biochemistry and Biophysics 218 (1982), 156–162.
    • (1982) Archives of Biochemistry and Biophysics , vol.218 , pp. 156-162
    • Bella, A.M.1    Erickson, R.H.2    Kim, Y.S.3
  • 9
    • 0002035994 scopus 로고
    • Screening methods for antibacterial and antiviral agents from higher plants
    • Berghe, V.A., Vlietinck, A.J., Screening methods for antibacterial and antiviral agents from higher plants. Methods for Plant Biochemistry 6 (1991), 47–68.
    • (1991) Methods for Plant Biochemistry , vol.6 , pp. 47-68
    • Berghe, V.A.1    Vlietinck, A.J.2
  • 11
    • 84942083434 scopus 로고    scopus 로고
    • Antimicrobial and antioxidant properties of the crude peptide extracts of Galatea paradoxa and Patella rustica
    • Borquaye, L.S., Darko, G., Ocansey, E., Ankomah, E., Antimicrobial and antioxidant properties of the crude peptide extracts of Galatea paradoxa and Patella rustica. SpringerPlus 4 (2015), 500–506.
    • (2015) SpringerPlus , vol.4 , pp. 500-506
    • Borquaye, L.S.1    Darko, G.2    Ocansey, E.3    Ankomah, E.4
  • 12
    • 0036004573 scopus 로고    scopus 로고
    • Structure and activity of angiotensin I-converting enzyme inhibitory peptides derived from Alaskan pollack skin
    • Byun, H.G., Kim, S.K., Structure and activity of angiotensin I-converting enzyme inhibitory peptides derived from Alaskan pollack skin. Journal of Biochemistry and Molecular Biology 35 (2002), 239–243.
    • (2002) Journal of Biochemistry and Molecular Biology , vol.35 , pp. 239-243
    • Byun, H.G.1    Kim, S.K.2
  • 16
    • 84861123585 scopus 로고    scopus 로고
    • Strand length-dependent antimicrobial activity and membrane active mechanism of arginine- and valine-rich β-hairpin-like antimicrobial peptides
    • Dong, N., Ma, Q., Shan, A., Lv, Y., Hu, W., Gu, Y. et al., Strand length-dependent antimicrobial activity and membrane active mechanism of arginine- and valine-rich β-hairpin-like antimicrobial peptides. Antimicrobial Agents and Chemotherapy 56 (2012), 2994–3003.
    • (2012) Antimicrobial Agents and Chemotherapy , vol.56 , pp. 2994-3003
    • Dong, N.1    Ma, Q.2    Shan, A.3    Lv, Y.4    Hu, W.5    Gu, Y.6
  • 17
    • 0031936324 scopus 로고    scopus 로고
    • Conformational and topological requirements of cell-permeable peptide function
    • Du, D.G., Yao, S.Y., Rojas, M., Lin, Y.Z., Conformational and topological requirements of cell-permeable peptide function. Journal of Peptide Research 51 (1998), 235–243.
    • (1998) Journal of Peptide Research , vol.51 , pp. 235-243
    • Du, D.G.1    Yao, S.Y.2    Rojas, M.3    Lin, Y.Z.4
  • 18
    • 0032439997 scopus 로고    scopus 로고
    • A sensitive and quick microplate method to determine the minimal inhibitory concentration of plant extracts for bacteria
    • Eloff, J.N., A sensitive and quick microplate method to determine the minimal inhibitory concentration of plant extracts for bacteria. Planta Medica 64 (1998), 711–713.
    • (1998) Planta Medica , vol.64 , pp. 711-713
    • Eloff, J.N.1
  • 19
    • 84930181095 scopus 로고    scopus 로고
    • Purification and characterization of four antibacterial peptides from protamex hydrolysate of Atlantic mackerel (Scomber scombrus) by-products
    • Ennaas, N., Hammami, R., Beaulieu, L., Fliss, I., Purification and characterization of four antibacterial peptides from protamex hydrolysate of Atlantic mackerel (Scomber scombrus) by-products. Biochemical and Biophysical Research Communications 462 (2015), 195–200.
    • (2015) Biochemical and Biophysical Research Communications , vol.462 , pp. 195-200
    • Ennaas, N.1    Hammami, R.2    Beaulieu, L.3    Fliss, I.4
  • 21
    • 84949434080 scopus 로고    scopus 로고
    • Angiotensin-I converting enzyme (ACE) inhibitory and anti-oxidant activities of sea cucumber (Actinopyga lecanora) hydrolysates
    • Ghanbari, R., Zarei, M., Ebrahimpour, A., Abdul-Hamid, A., Ismail, A., Saari, N., Angiotensin-I converting enzyme (ACE) inhibitory and anti-oxidant activities of sea cucumber (Actinopyga lecanora) hydrolysates. International Journal of Molecular Sciences 16 (2015), 28870–28885.
    • (2015) International Journal of Molecular Sciences , vol.16 , pp. 28870-28885
    • Ghanbari, R.1    Zarei, M.2    Ebrahimpour, A.3    Abdul-Hamid, A.4    Ismail, A.5    Saari, N.6
  • 22
    • 0033823597 scopus 로고    scopus 로고
    • Production of angiotensin-I-converting-enzyme-inhibitory peptides in fermented milks started by Lactobacillus delbrueckii subsp. bulgaricus SS1 and Lactococcus lactis subsp. cremoris FT4
    • Gobbetti, M., Ferranti, P., Smacchi, E., Goffredi, F., Addeo, F., Production of angiotensin-I-converting-enzyme-inhibitory peptides in fermented milks started by Lactobacillus delbrueckii subsp. bulgaricus SS1 and Lactococcus lactis subsp. cremoris FT4. Applied and Environmental Microbiology 66 (2000), 3898–3904.
    • (2000) Applied and Environmental Microbiology , vol.66 , pp. 3898-3904
    • Gobbetti, M.1    Ferranti, P.2    Smacchi, E.3    Goffredi, F.4    Addeo, F.5
  • 23
    • 79957674334 scopus 로고    scopus 로고
    • An enzyme sensor for the determination of total amines in dry-fermented sausages
    • Hernández-Cázares, A., Aristoy, M.C., Toldrá, F., An enzyme sensor for the determination of total amines in dry-fermented sausages. Journal of Food Engineering 106 (2011), 166–169.
    • (2011) Journal of Food Engineering , vol.106 , pp. 166-169
    • Hernández-Cázares, A.1    Aristoy, M.C.2    Toldrá, F.3
  • 24
    • 0012543842 scopus 로고    scopus 로고
    • The role of vascular biology, nutrition and nutraceuticals in the prevention and treatment of hypertension
    • Houston, M.C., The role of vascular biology, nutrition and nutraceuticals in the prevention and treatment of hypertension. Journal of the American Nutraceutical Association Suppl. No. I (2002), 1–71.
    • (2002) Journal of the American Nutraceutical Association , vol.Suppl. No. I , pp. 1-71
    • Houston, M.C.1
  • 25
    • 84954305765 scopus 로고    scopus 로고
    • Antioxidant and antibacterial activities of peptide fractions from flaxseed protein hydrolysed by protease from Bacillus altitudinis HK02
    • Hwang, C.-F., Chen, Y.-A., Luo, C., Chiang, X.-D., Antioxidant and antibacterial activities of peptide fractions from flaxseed protein hydrolysed by protease from Bacillus altitudinis HK02. International Journal of Food Science and Technology 51 (2016), 681–689.
    • (2016) International Journal of Food Science and Technology , vol.51 , pp. 681-689
    • Hwang, C.-F.1    Chen, Y.-A.2    Luo, C.3    Chiang, X.-D.4
  • 26
    • 84872106766 scopus 로고    scopus 로고
    • Selective antimicrobial activity and mode of action of adepantins, glycine-rich peptide antibiotics based on anuran antimicrobial peptide sequences
    • Ilić, N., Novković, M., Guida, F., Xhindoli, D., Benincasa, M., Tossi, A. et al., Selective antimicrobial activity and mode of action of adepantins, glycine-rich peptide antibiotics based on anuran antimicrobial peptide sequences. Biochimica et Biophysica Acta 1828 (2013), 1004–1412.
    • (2013) Biochimica et Biophysica Acta , vol.1828 , pp. 1004-1412
    • Ilić, N.1    Novković, M.2    Guida, F.3    Xhindoli, D.4    Benincasa, M.5    Tossi, A.6
  • 27
    • 34848813865 scopus 로고    scopus 로고
    • Antioxidant peptide isolated from muscle protein of bullfrog, Rana catesbeiana Shaw
    • Je, J.Y., Qian, Z.J., Kim, S.K., Antioxidant peptide isolated from muscle protein of bullfrog, Rana catesbeiana Shaw. Journal of Medicinal Food 10 (2007), 401–407.
    • (2007) Journal of Medicinal Food , vol.10 , pp. 401-407
    • Je, J.Y.1    Qian, Z.J.2    Kim, S.K.3
  • 28
    • 85002940310 scopus 로고    scopus 로고
    • Peptidomic analysis of bioactive peptides in zebra blenny (Salaria basilisca) muscle protein hydrolysate exhibiting antimicrobial activity obtained by fermentation with Bacillus mojavensis A21
    • Jemil, I., Abdelhedi, O., Mora, L., Nasri, R., Aristoy, M.C., Jridi, M. et al., Peptidomic analysis of bioactive peptides in zebra blenny (Salaria basilisca) muscle protein hydrolysate exhibiting antimicrobial activity obtained by fermentation with Bacillus mojavensis A21. Process Biochemistry 51 (2016), 2186–2197.
    • (2016) Process Biochemistry , vol.51 , pp. 2186-2197
    • Jemil, I.1    Abdelhedi, O.2    Mora, L.3    Nasri, R.4    Aristoy, M.C.5    Jridi, M.6
  • 29
    • 84899952227 scopus 로고    scopus 로고
    • Functional, antioxidant and antibacterial properties of protein hydrolysates prepared from fish meat fermented by Bacillus subtilis A26
    • Jemil, I., Jridi, M., Nasri, R., Ktari, N., Ben Slama-Ben Salem, R., Mehiri, M. et al., Functional, antioxidant and antibacterial properties of protein hydrolysates prepared from fish meat fermented by Bacillus subtilis A26. Process Biochemistry 49 (2014), 963–972.
    • (2014) Process Biochemistry , vol.49 , pp. 963-972
    • Jemil, I.1    Jridi, M.2    Nasri, R.3    Ktari, N.4    Ben Slama-Ben Salem, R.5    Mehiri, M.6
  • 30
    • 84994462243 scopus 로고    scopus 로고
    • A peptidomic approach for the identification of antioxidant and ACE-inhibitory peptides in sardinelle protein hydrolysates fermented by Bacillus subtilis A26 and Bacillus amyloliquefaciens An6
    • Jemil, I., Mora, L., Nasri, R., Abdelhedi, O., Aristoy, M.C., Hajji, M. et al., A peptidomic approach for the identification of antioxidant and ACE-inhibitory peptides in sardinelle protein hydrolysates fermented by Bacillus subtilis A26 and Bacillus amyloliquefaciens An6. Food Research International 89 (2016), 347–358.
    • (2016) Food Research International , vol.89 , pp. 347-358
    • Jemil, I.1    Mora, L.2    Nasri, R.3    Abdelhedi, O.4    Aristoy, M.C.5    Hajji, M.6
  • 31
    • 0027352759 scopus 로고
    • Salt-tolerant and thermostable alkaline protease from Bacillus subtilis NCIM no. 64
    • Kembhavi, A.A., Kulkarni, A., Pant, A., Salt-tolerant and thermostable alkaline protease from Bacillus subtilis NCIM no. 64. Applied Biochemistry and Biotechnology 38 (1993), 3–92.
    • (1993) Applied Biochemistry and Biotechnology , vol.38 , pp. 3-92
    • Kembhavi, A.A.1    Kulkarni, A.2    Pant, A.3
  • 32
  • 33
    • 77951713273 scopus 로고    scopus 로고
    • Advanced taste sensors based on artificial lipids with global selectivity to basic taste qualities and high correlation to sensory scores
    • Kobayashi, Y., Habara, M., Ikezazki, H., Chen, R., Naito, Y., Toko, K., Advanced taste sensors based on artificial lipids with global selectivity to basic taste qualities and high correlation to sensory scores. Sensors 10 (2010), 3411–3443.
    • (2010) Sensors , vol.10 , pp. 3411-3443
    • Kobayashi, Y.1    Habara, M.2    Ikezazki, H.3    Chen, R.4    Naito, Y.5    Toko, K.6
  • 34
    • 85028526196 scopus 로고    scopus 로고
    • Antibacterial and antioxidant activities of goat milk hydrolysate generated by Bacillus sp. E.13
    • Kusumaningtyas, E., Widiastuti, R., Kusumaningrum, H.D., Suhartono, M.T., Antibacterial and antioxidant activities of goat milk hydrolysate generated by Bacillus sp. E.13. Global Veterinaria 16 (2016), 105–110.
    • (2016) Global Veterinaria , vol.16 , pp. 105-110
    • Kusumaningtyas, E.1    Widiastuti, R.2    Kusumaningrum, H.D.3    Suhartono, M.T.4
  • 35
    • 84945463197 scopus 로고    scopus 로고
    • Characterization, antioxidative and ACE inhibitory properties of hydrolysates obtained from thornback ray (Raja clavata) muscle
    • Lassoued, I., Mora, L., Nasri, R., Aydi, M., Toldrá, F., Aristoy, M.C. et al., Characterization, antioxidative and ACE inhibitory properties of hydrolysates obtained from thornback ray (Raja clavata) muscle. Journal of Proteomics 128 (2015), 458–468.
    • (2015) Journal of Proteomics , vol.128 , pp. 458-468
    • Lassoued, I.1    Mora, L.2    Nasri, R.3    Aydi, M.4    Toldrá, F.5    Aristoy, M.C.6
  • 36
    • 0037901037 scopus 로고    scopus 로고
    • Minireview: Overview of the renin-angiotensin system; An endocrine and paracrine system
    • Lavoie, J.L., Sigmund, C.D., Minireview: Overview of the renin-angiotensin system; An endocrine and paracrine system. Endocrinology 144 (2003), 2179–2183.
    • (2003) Endocrinology , vol.144 , pp. 2179-2183
    • Lavoie, J.L.1    Sigmund, C.D.2
  • 38
    • 0036215877 scopus 로고    scopus 로고
    • Effect of antioxidants on the oxidative stability of chicken breast meat in a dispersion system
    • Lin, C.C., Liang, J.H., Effect of antioxidants on the oxidative stability of chicken breast meat in a dispersion system. Journal of Food Science 67 (2002), 530–533.
    • (2002) Journal of Food Science , vol.67 , pp. 530-533
    • Lin, C.C.1    Liang, J.H.2
  • 39
    • 84905020130 scopus 로고    scopus 로고
    • Rapid identification of bioactive peptides with antioxidant activity from the enzymatic hydrolysate of Mactra veneriformis by UHPLC–Q-TOF mass spectrometry
    • Liu, R., Zheng, W., Li, J., Wang, L., Wu, H., Wang, X., Shi, L., Rapid identification of bioactive peptides with antioxidant activity from the enzymatic hydrolysate of Mactra veneriformis by UHPLC–Q-TOF mass spectrometry. Food Chemistry 167 (2015), 484–489.
    • (2015) Food Chemistry , vol.167 , pp. 484-489
    • Liu, R.1    Zheng, W.2    Li, J.3    Wang, L.4    Wu, H.5    Wang, X.6    Shi, L.7
  • 40
    • 84869862833 scopus 로고    scopus 로고
    • Purification and characterization of angiotensin I converting enzyme inhibitory peptides from jellyfish Rhopilema esculentun
    • Liu, X., Zhang, M., Jia, A., Zhang, Y., Zhu, H., Zhang, C. et al., Purification and characterization of angiotensin I converting enzyme inhibitory peptides from jellyfish Rhopilema esculentun. Food Research International 50 (2013), 339–343.
    • (2013) Food Research International , vol.50 , pp. 339-343
    • Liu, X.1    Zhang, M.2    Jia, A.3    Zhang, Y.4    Zhu, H.5    Zhang, C.6
  • 41
    • 3142754252 scopus 로고    scopus 로고
    • Angiotensin converting enzyme inhibitory peptides in Finnish cereals: A data base survey
    • Loponen, J., Angiotensin converting enzyme inhibitory peptides in Finnish cereals: A data base survey. Agricultural and Food Science 13 (2004), 39–45.
    • (2004) Agricultural and Food Science , vol.13 , pp. 39-45
    • Loponen, J.1
  • 42
    • 0023218568 scopus 로고
    • Studies on the active site and antihypertensive activity of angiotensin I-converting enzyme inhibitors derived from casein
    • Maruyama, S., Mitachi, H., Tanaka, H., Tomizuka, N., Suzuki, H., Studies on the active site and antihypertensive activity of angiotensin I-converting enzyme inhibitors derived from casein. Agricultural and Biological Chemistry 51 (1987), 1581–1586.
    • (1987) Agricultural and Biological Chemistry , vol.51 , pp. 1581-1586
    • Maruyama, S.1    Mitachi, H.2    Tanaka, H.3    Tomizuka, N.4    Suzuki, H.5
  • 43
    • 0027228287 scopus 로고
    • Inhibitory effects of enzymatic hydrolysates of collagen and collagen-relatedsynthetic peptides on fibrinogen/thrombin clotting
    • Maruyama, S., Nonaka, I., Tanaka, H., Inhibitory effects of enzymatic hydrolysates of collagen and collagen-relatedsynthetic peptides on fibrinogen/thrombin clotting. Biochimica et Biophysica Acta 1164 (1993), 215–218.
    • (1993) Biochimica et Biophysica Acta , vol.1164 , pp. 215-218
    • Maruyama, S.1    Nonaka, I.2    Tanaka, H.3
  • 44
    • 0032076817 scopus 로고    scopus 로고
    • Overview on milk protein-derived peptides
    • Meisel, H., Overview on milk protein-derived peptides. International Dairy Journal 8 (1998), 363–373.
    • (1998) International Dairy Journal , vol.8 , pp. 363-373
    • Meisel, H.1
  • 46
    • 0026161547 scopus 로고
    • Structure and activity of angiotensin-converting enzyme inhibitors in alpha-zein hydrolysate
    • Miyoshi, S., Ishikawa, H., Kaneko, T., Fukui, F., Tanaka, H., Structure and activity of angiotensin-converting enzyme inhibitors in alpha-zein hydrolysate. Agricultural and Biological Chemistry 55 (1991), 1313–1318.
    • (1991) Agricultural and Biological Chemistry , vol.55 , pp. 1313-1318
    • Miyoshi, S.1    Ishikawa, H.2    Kaneko, T.3    Fukui, F.4    Tanaka, H.5
  • 47
    • 84940451563 scopus 로고    scopus 로고
    • A peptidomic approach to study the contribution of added casein proteins to the peptide profile in Spanish dry-fermented sausages
    • Mora, L., Escudero, E., Aristoy, M.C., Toldrá, F., A peptidomic approach to study the contribution of added casein proteins to the peptide profile in Spanish dry-fermented sausages. International Journal of Food Microbiology 212 (2015), 41–48.
    • (2015) International Journal of Food Microbiology , vol.212 , pp. 41-48
    • Mora, L.1    Escudero, E.2    Aristoy, M.C.3    Toldrá, F.4
  • 48
    • 84882767015 scopus 로고    scopus 로고
    • ACE inhibitory and antioxidative activities of goby (Zosterissessor ophiocephalus) fish protein hydrolysates: Effect on meat lipid oxidation
    • Nasri, R., Younes, I., Jridi, M., Trigui, M., Bougatef, A., Nedjar-Arroume, N. et al., ACE inhibitory and antioxidative activities of goby (Zosterissessor ophiocephalus) fish protein hydrolysates: Effect on meat lipid oxidation. Food Research International 54 (2013), 552–561.
    • (2013) Food Research International , vol.54 , pp. 552-561
    • Nasri, R.1    Younes, I.2    Jridi, M.3    Trigui, M.4    Bougatef, A.5    Nedjar-Arroume, N.6
  • 49
    • 0029030898 scopus 로고
    • Structure-activity study of a laminin alpha 1 chain active peptide sgment Ile-Lys-Val-Ala-Val (IKVAV)
    • Nomizu, M., Week, B.S., Weston, C.A., Kim, W.H., Kleinman, H.K., Yamada, Y., Structure-activity study of a laminin alpha 1 chain active peptide sgment Ile-Lys-Val-Ala-Val (IKVAV). FEBS Letters 365 (1995), 227–231.
    • (1995) FEBS Letters , vol.365 , pp. 227-231
    • Nomizu, M.1    Week, B.S.2    Weston, C.A.3    Kim, W.H.4    Kleinman, H.K.5    Yamada, Y.6
  • 50
    • 84901310564 scopus 로고    scopus 로고
    • In silico approaches to predict the potential of milk protein-derived peptides as dipeptidyl peptidase IV (DPP-IV) inhibitors
    • Nongonierma, A.B., Mooney, C., Shields, D.C., FitzGerald, R.J., In silico approaches to predict the potential of milk protein-derived peptides as dipeptidyl peptidase IV (DPP-IV) inhibitors. Peptides 57 (2014), 43–51.
    • (2014) Peptides , vol.57 , pp. 43-51
    • Nongonierma, A.B.1    Mooney, C.2    Shields, D.C.3    FitzGerald, R.J.4
  • 51
    • 0036633301 scopus 로고    scopus 로고
    • The short proline-rich antibacterial peptide family
    • Otvos, L., The short proline-rich antibacterial peptide family. Cellular and Molecular Life Sciences 59 (2002), 1138–1150.
    • (2002) Cellular and Molecular Life Sciences , vol.59 , pp. 1138-1150
    • Otvos, L.1
  • 52
    • 34748844591 scopus 로고    scopus 로고
    • Antimicrobial peptides: Natural effectors of the innate immune system
    • Radek, K., Gallo, R., Antimicrobial peptides: Natural effectors of the innate immune system. Seminars in Immunopathology 29 (2007), 27–43.
    • (2007) Seminars in Immunopathology , vol.29 , pp. 27-43
    • Radek, K.1    Gallo, R.2
  • 53
    • 0028339191 scopus 로고
    • Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes: Facets of their conformational features, structure-function correlations and membrane-perturbing abilities
    • Saberwal, G., Nagaraj, R., Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes: Facets of their conformational features, structure-function correlations and membrane-perturbing abilities. Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes 1197 (1994), 109–131.
    • (1994) Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes , vol.1197 , pp. 109-131
    • Saberwal, G.1    Nagaraj, R.2
  • 54
    • 3242718855 scopus 로고    scopus 로고
    • From bedside to bench to bedside: Role of renin-angiotensin-aldosterone system in remodeling of resistance arteries in hypertension
    • Schiffrin, E.L., Touyz, R.M., From bedside to bench to bedside: Role of renin-angiotensin-aldosterone system in remodeling of resistance arteries in hypertension. American Journal of Physiology Heart and Circulatory Physiology 287 (2004), 435–446.
    • (2004) American Journal of Physiology Heart and Circulatory Physiology , vol.287 , pp. 435-446
    • Schiffrin, E.L.1    Touyz, R.M.2
  • 55
    • 29344434264 scopus 로고    scopus 로고
    • A rapid, simple and sensitive fluorescence method for the assay of angiotensin-I converting enzyme
    • Sentandreu, M.A., Toldrá, F., A rapid, simple and sensitive fluorescence method for the assay of angiotensin-I converting enzyme. Food Chemistry 97 (2006), 546–554.
    • (2006) Food Chemistry , vol.97 , pp. 546-554
    • Sentandreu, M.A.1    Toldrá, F.2
  • 58
    • 0029956552 scopus 로고    scopus 로고
    • Antibacterial activity of glycosylated and phosphorylated chromogranin A-derived peptide 173–194 from bovine adrenal medullary chromaffin granules
    • Strub, J.M., Goumon, Y., Lugardon, K., Capon, C., Lopez, M., Moniatte, M., Metz-Boutigue, M.H., Antibacterial activity of glycosylated and phosphorylated chromogranin A-derived peptide 173–194 from bovine adrenal medullary chromaffin granules. Journal of Biological Chemistry 271 (1996), 28533–28540.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 28533-28540
    • Strub, J.M.1    Goumon, Y.2    Lugardon, K.3    Capon, C.4    Lopez, M.5    Moniatte, M.6    Metz-Boutigue, M.H.7
  • 59
    • 84944327213 scopus 로고    scopus 로고
    • Preparation of potent antioxidant peptide from edible part of shortclub cuttlefish against radical mediated lipid and DNA damage
    • Sudhakar, S., Abdul Nazeer, R., Preparation of potent antioxidant peptide from edible part of shortclub cuttlefish against radical mediated lipid and DNA damage. LWT - Food Science and Technology 64 (2015), 593–601.
    • (2015) LWT - Food Science and Technology , vol.64 , pp. 593-601
    • Sudhakar, S.1    Abdul Nazeer, R.2
  • 61
    • 0011900648 scopus 로고
    • Biochemical basis of postmortem nucleotide catabolism in cod (Gadus morhua) and its relationship to spoilage
    • Surette, M.E., Gill, T.A., LeBlanc, P.J., Biochemical basis of postmortem nucleotide catabolism in cod (Gadus morhua) and its relationship to spoilage. Journal of Agricultural and Food Chemistry 36 (1988), 19–22.
    • (1988) Journal of Agricultural and Food Chemistry , vol.36 , pp. 19-22
    • Surette, M.E.1    Gill, T.A.2    LeBlanc, P.J.3
  • 62
    • 84904962611 scopus 로고    scopus 로고
    • Targeted separation of antibacterial peptide from protein hydrolysate of anchovy cooking wastewater by equilibrium dialysis
    • Tang, W., Zhang, H., Wang, L., Qian, H., Qi, X., Targeted separation of antibacterial peptide from protein hydrolysate of anchovy cooking wastewater by equilibrium dialysis. Food Chemistry 168 (2015), 115–123.
    • (2015) Food Chemistry , vol.168 , pp. 115-123
    • Tang, W.1    Zhang, H.2    Wang, L.3    Qian, H.4    Qi, X.5
  • 63
    • 84866782465 scopus 로고    scopus 로고
    • Novel angiotensin I-converting enzyme inhibitory peptides derived from soya milk
    • Tomatsu, M., Shimakage, A., Shinbo, M., Yamada, S., Takahashi, S., Novel angiotensin I-converting enzyme inhibitory peptides derived from soya milk. Food Chemistry 136 (2013), 612–616.
    • (2013) Food Chemistry , vol.136 , pp. 612-616
    • Tomatsu, M.1    Shimakage, A.2    Shinbo, M.3    Yamada, S.4    Takahashi, S.5
  • 64
    • 84856032752 scopus 로고    scopus 로고
    • Food protein-derived bioactive peptides: Production, processing, and potential health benefits
    • Udenigwe, C.C., Aluko, R.E., Food protein-derived bioactive peptides: Production, processing, and potential health benefits. Journal of Food Science 71 (2012), R11–R24.
    • (2012) Journal of Food Science , vol.71 , pp. R11-R24
    • Udenigwe, C.C.1    Aluko, R.E.2
  • 66
    • 0030721013 scopus 로고    scopus 로고
    • Influence of the angle subtended by the positively charged helix face on the membrane activity of amphipathic, antibacterial peptides
    • Wieprecht, T., Dathe, M., Epand, R.M., Beyermann, M., Krause, E., Maloy, W.L. et al., Influence of the angle subtended by the positively charged helix face on the membrane activity of amphipathic, antibacterial peptides. Biochemistry 36 (1997), 12869–12880.
    • (1997) Biochemistry , vol.36 , pp. 12869-12880
    • Wieprecht, T.1    Dathe, M.2    Epand, R.M.3    Beyermann, M.4    Krause, E.5    Maloy, W.L.6
  • 67
    • 0034845022 scopus 로고    scopus 로고
    • Determination of antioxidant and antimicrobial activities of Rumex crispus L. extracts
    • Yildirim, A., Mavi, A., Kara, A.A., Determination of antioxidant and antimicrobial activities of Rumex crispus L. extracts. Journal of Agricultural and Food Chemistry 49 (2001), 4083–4089.
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , pp. 4083-4089
    • Yildirim, A.1    Mavi, A.2    Kara, A.A.3
  • 68
    • 70349916047 scopus 로고    scopus 로고
    • Antioxidant activities of the rice endosperm protein hydrolysate: Identification of the active peptide
    • Zhang, J., Zhang, H., Wang, L., Guo, H., Wang, X., Yao, H., Antioxidant activities of the rice endosperm protein hydrolysate: Identification of the active peptide. European Food Research and Technology 229 (2009), 709–719.
    • (2009) European Food Research and Technology , vol.229 , pp. 709-719
    • Zhang, J.1    Zhang, H.2    Wang, L.3    Guo, H.4    Wang, X.5    Yao, H.6
  • 69
    • 43649092437 scopus 로고    scopus 로고
    • Reducing, radical scavenging, and chelation properties of in vitro digests of alcalase-treated zein hydrolysate
    • Zhu, L., Chen, J., Tang, X., Xiong, Y.B., 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, J.2    Tang, X.3    Xiong, Y.B.4
  • 70
    • 85000869948 scopus 로고    scopus 로고
    • The structure-activity relationship of the antioxidant peptides from natural proteins
    • Zou, T.B., He, T.P., Li, H.B., Tang, H.W., Xia, E.Q., The structure-activity relationship of the antioxidant peptides from natural proteins. Molecules 21 (2016), 1–14.
    • (2016) Molecules , vol.21 , pp. 1-14
    • Zou, T.B.1    He, T.P.2    Li, H.B.3    Tang, H.W.4    Xia, E.Q.5


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