메뉴 건너뛰기




Volumn 60, Issue 22, 2012, Pages 5636-5643

Production of porcine hemoglobin peptides at moderate temperature and medium pressure under a nitrogen stream. Functional and antioxidant properties

Author keywords

antioxidant properties; functional properties; nonenzymatic hydrolysis; porcine hemoglobin

Indexed keywords

ANTIOXIDANT PROPERTIES; AVERAGE SIZE; FUNCTIONAL PROPERTIES; HIGH HYDROSTATIC PRESSURE; MEDIUM PRESSURE; MODERATE TEMPERATURE; NONENZYMATIC HYDROLYSIS;

EID: 84861886358     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf300400k     Document Type: Article
Times cited : (45)

References (37)
  • 1
    • 0030809336 scopus 로고    scopus 로고
    • Preliminary studies on the processing of slaughter-house blood for protein recovery
    • Rendueles, M.; Moure, F.; Fernández, A.; Díaz, M. Preliminary studies on the processing of slaughter-house blood for protein recovery Resour. Environ. Biotechnol. 1997, 1, 193-206
    • (1997) Resour. Environ. Biotechnol. , vol.1 , pp. 193-206
    • Rendueles, M.1    Moure, F.2    Fernández, A.3    Díaz, M.4
  • 3
    • 0036222796 scopus 로고    scopus 로고
    • Process development for heme-enriched peptide by enzymatic hydrolysis of hemoglobin
    • In, M.-J.; Chae, J. H.; Oh, N.-S. Process development for heme-enriched peptide by enzymatic hydrolysis of hemoglobin Bioresour. Technol. 2002, 84, 63-68
    • (2002) Bioresour. Technol. , vol.84 , pp. 63-68
    • In, M.-J.1    Chae, J.H.2    Oh, N.-S.3
  • 4
    • 0037077396 scopus 로고    scopus 로고
    • Influence of the extent of hemoglobin hydrolysis on the digestive absorption of heme iron. An in vitro study
    • Vaghefi, N.; Fouzia, N.; Guillochon, D.; Bureau, F.; Arhan, P.; Bouglé, D. Influence of the extent of hemoglobin hydrolysis on the digestive absorption of heme iron. An in vitro study J. Agric. Food Chem. 2002, 50, 4969-4973
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 4969-4973
    • Vaghefi, N.1    Fouzia, N.2    Guillochon, D.3    Bureau, F.4    Arhan, P.5    Bouglé, D.6
  • 6
    • 33746725357 scopus 로고    scopus 로고
    • Antioxidant properties and protein compositions of porcine haemoglobin hydrolysis
    • Chang, C.-Y.; Wu, K.-C.; Chiang, S.-H. Antioxidant properties and protein compositions of porcine haemoglobin hydrolysis Food Chem. 2007, 100, 1537-1543
    • (2007) Food Chem. , vol.100 , pp. 1537-1543
    • Chang, C.-Y.1    Wu, K.-C.2    Chiang, S.-H.3
  • 7
    • 58249140350 scopus 로고    scopus 로고
    • Purification of an iron-binding nona-peptide from hydrolysates of porcine blood plasma protein
    • Lee, S.-H.; Song, K. B. Purification of an iron-binding nona-peptide from hydrolysates of porcine blood plasma protein Process Biochem. (Oxford) 2009, 44, 378-381
    • (2009) Process Biochem. (Oxford) , vol.44 , pp. 378-381
    • Lee, S.-H.1    Song, K.B.2
  • 8
    • 33750041097 scopus 로고    scopus 로고
    • Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides derived from porcine hemoglobin
    • Yike, Yu, Y.; Hua, J.; Miyaguchi, Y.; Bai, X.; Dua, Y.; Lin, B. Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides derived from porcine hemoglobin Peptides 2006, 27, 2950-2956
    • (2006) Peptides , vol.27 , pp. 2950-2956
    • Yike, Y.Y.1    Hua, J.2    Miyaguchi, Y.3    Bai, X.4    Dua, Y.5    Lin, B.6
  • 9
    • 77951232062 scopus 로고    scopus 로고
    • Sub-critical water hydrolysis of hog hair for amino acid production
    • Esteban, M. B.; García, A. J.; Ramos, P.; Márquez, M. C. Sub-critical water hydrolysis of hog hair for amino acid production Bioresour. Technol. 2010, 101, 2472-2476
    • (2010) Bioresour. Technol. , vol.101 , pp. 2472-2476
    • Esteban, M.B.1    García, A.J.2    Ramos, P.3    Márquez, M.C.4
  • 10
    • 24944527953 scopus 로고    scopus 로고
    • Production of amino acids from bovine serum albumin by continuous sub-critical water hydrolysis
    • Rogalinski, T.; Herrmann, S.; Brunner, G. Production of amino acids from bovine serum albumin by continuous sub-critical water hydrolysis J. Supercrit. Fluids 2005, 36, 49-58
    • (2005) J. Supercrit. Fluids , vol.36 , pp. 49-58
    • Rogalinski, T.1    Herrmann, S.2    Brunner, G.3
  • 11
    • 45949092407 scopus 로고    scopus 로고
    • Amino acids production from fish proteins hydrolysis in subcritical water
    • Xian, Z.; Chao, Z.; Liang, Z.; Cheng, H. Amino acids production from fish proteins hydrolysis in subcritical water Chin. J. Chem. Eng. 2008, 16, 456-460
    • (2008) Chin. J. Chem. Eng. , vol.16 , pp. 456-460
    • Xian, Z.1    Chao, Z.2    Liang, Z.3    Cheng, H.4
  • 12
    • 80054052128 scopus 로고    scopus 로고
    • Hemoglobin hydrolysates from porcine blood obtained through enzymatic hydrolysis assisted by high hydrostatic pressure processing
    • Toldrá, M.; Parés, D.; Saguer, E.; Carretero, C. Hemoglobin hydrolysates from porcine blood obtained through enzymatic hydrolysis assisted by high hydrostatic pressure processing Innovative Food Sci. Emerging Technol. 2011, 12, 435-442
    • (2011) Innovative Food Sci. Emerging Technol. , vol.12 , pp. 435-442
    • Toldrá, M.1    Parés, D.2    Saguer, E.3    Carretero, C.4
  • 13
    • 34249093940 scopus 로고    scopus 로고
    • The use of high hydrostatic pressure to promote the proteolysis and release of bioactive peptides from ovalbumin
    • Quirós, A.; Chichón, R.; Recio, I.; López- Fandiño, R. The use of high hydrostatic pressure to promote the proteolysis and release of bioactive peptides from ovalbumin Food Chem. 2007, 104, 1734-1739
    • (2007) Food Chem. , vol.104 , pp. 1734-1739
    • Quirós, A.1    Chichón, R.2    Recio, I.3    López-Fandiño, R.4
  • 15
    • 0037171132 scopus 로고    scopus 로고
    • Pressure-temperature phase diagrams of biomolecules
    • Smeller, L. Pressure-temperature phase diagrams of biomolecules Biochim. Biophys. Acta 2002, 1595, 11-29
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 11-29
    • Smeller, L.1
  • 16
    • 0036747380 scopus 로고    scopus 로고
    • High-pressure as a tool to study some proteins' properties, conformational modification, activity and oligomeric dissociation
    • Lullien-Pellerin, V.; Balny, C. High-pressure as a tool to study some proteins' properties, conformational modification, activity and oligomeric dissociation Innovative Food Sci. Emerging Technol. 2002, 3, 209-221
    • (2002) Innovative Food Sci. Emerging Technol. , vol.3 , pp. 209-221
    • Lullien-Pellerin, V.1    Balny, C.2
  • 18
    • 0035096518 scopus 로고    scopus 로고
    • Enzymatic protein hydrolysates in human nutrition
    • Clemente, A. Enzymatic protein hydrolysates in human nutrition Trends Food Sci. Technol. 2000, 11, 254-262
    • (2000) Trends Food Sci. Technol. , vol.11 , pp. 254-262
    • Clemente, A.1
  • 19
    • 0022900156 scopus 로고
    • High performance size exclusion liquid chromatography of small molecular weight peptides from protein hydrolysates using methanol as a mobile phase additive
    • Vijayalakshmi, M. A.; Lemieux, L.; Amoit, J. High performance size exclusion liquid chromatography of small molecular weight peptides from protein hydrolysates using methanol as a mobile phase additive J. Liq. Chromatogr. 1986, 9, 3559-3576
    • (1986) J. Liq. Chromatogr. , vol.9 , pp. 3559-3576
    • Vijayalakshmi, M.A.1    Lemieux, L.2    Amoit, J.3
  • 20
    • 0006289897 scopus 로고
    • Digestible amino acids for non-ruminant animals, theory and recent challenges
    • Williams, P. E. V. Digestible amino acids for non-ruminant animals, theory and recent challenges Anim. Feed Sci Technol. 1995, 53, 173-187
    • (1995) Anim. Feed Sci Technol. , vol.53 , pp. 173-187
    • Williams, P.E.V.1
  • 22
    • 51749125669 scopus 로고    scopus 로고
    • Antioxidant activity of peptides isolated from alfalfa leaf protein hydrolysate
    • Xie, Z.; Huang, J.; Xu, X.; Jin, X. Antioxidant activity of peptides isolated from alfalfa leaf protein hydrolysate Food Chem. 2008, 111, 370-376
    • (2008) Food Chem. , vol.111 , pp. 370-376
    • Xie, Z.1    Huang, J.2    Xu, X.3    Jin, X.4
  • 23
    • 49749221698 scopus 로고
    • A modified ninhydrin colorimetric analysis for amino acids
    • Rosen, H. A modified ninhydrin colorimetric analysis for amino acids Arch. Biochem. Biophys. 1957, 67, 10-15
    • (1957) Arch. Biochem. Biophys. , vol.67 , pp. 10-15
    • Rosen, H.1
  • 24
    • 84991134070 scopus 로고
    • Functional properties and amino acid content of a protein isolate from mung bean flour
    • Coffman, C; García, V. Functional properties and amino acid content of a protein isolate from mung bean flour J. Food Technol. 1977, 12, 473-484
    • (1977) J. Food Technol. , vol.12 , pp. 473-484
    • Coffman, C.1    García, V.2
  • 25
    • 2342438817 scopus 로고    scopus 로고
    • Rheology and microstructure of heat induced egg yolk gels
    • Cordobés, F.; Partal, P.; Guerrero, A. Rheology and microstructure of heat induced egg yolk gels Rheol. Acta 2004, 43, 184-195
    • (2004) Rheol. Acta , vol.43 , pp. 184-195
    • Cordobés, F.1    Partal, P.2    Guerrero, A.3
  • 26
    • 33847124120 scopus 로고    scopus 로고
    • Heat-Induced gelation of porcine blood plasma proteins as affected by pH
    • Dávila, E.; Parés, D.; Cuvelier, G.; Relkin, P. Heat-Induced gelation of porcine blood plasma proteins as affected by pH Meat Sci. 2006, 76, 216-225
    • (2006) Meat Sci. , vol.76 , pp. 216-225
    • Dávila, E.1    Parés, D.2    Cuvelier, G.3    Relkin, P.4
  • 27
    • 0000561073 scopus 로고
    • Determining the emulsifying and emulsion stabilizing capacity of protein meta additives
    • Inklaar, P. A.; Fortuin, J. Determining the emulsifying and emulsion stabilizing capacity of protein meta additives J. Food Technol. 1969, 23, 103-107
    • (1969) J. Food Technol. , vol.23 , pp. 103-107
    • Inklaar, P.A.1    Fortuin, J.2
  • 28
    • 56249120268 scopus 로고    scopus 로고
    • Recycling of oily ultrafiltration permeates to reformulate O/W emulsions
    • Matos, M.; Lobo, A.; Fernández, E.; Benito, J. M.; Pazos, C. Recycling of oily ultrafiltration permeates to reformulate O/W emulsions Colloids Surf., A 2008, 1-2, 8-15
    • (2008) Colloids Surf., A , vol.12 , pp. 8-15
    • Matos, M.1    Lobo, A.2    Fernández, E.3    Benito, J.M.4    Pazos, C.5
  • 29
    • 0345170751 scopus 로고
    • Antioxidant activity of various tea extracts in relation to their antimutagenicity
    • Yen, G. C.; Chen, H. Y. Antioxidant activity of various tea extracts in relation to their antimutagenicity J. Agric. Food Chem. 1995, 43, 27-32
    • (1995) J. Agric. Food Chem. , vol.43 , pp. 27-32
    • Yen, G.C.1    Chen, H.Y.2
  • 30
    • 9544245029 scopus 로고
    • Effects of Ge-132 on oxygen free radicals and the lipid peroxidation induced by hydroxyl free radical in vitro
    • Wang, J. C.; Xing, G. S.; Hu, W. D.; Zhu, T. L.; Wang, Q.; Zhao, H. Effects of Ge-132 on oxygen free radicals and the lipid peroxidation induced by hydroxyl free radical in vitro Chin. Pharm. J. 1994, 29, 23-25
    • (1994) Chin. Pharm. J. , vol.29 , pp. 23-25
    • Wang, J.C.1    Xing, G.S.2    Hu, W.D.3    Zhu, T.L.4    Wang, Q.5    Zhao, H.6
  • 31
    • 0028076361 scopus 로고
    • Action of phenolic derivates (acetoaminophen, salycilate and 5-aminosalycilate) as inhibitors of membrane lipid peroxidation and as peroxyl radical scavengers
    • Dinis, T. C. P.; Madeira, V. M. C.; Almeida, L. M. Action of phenolic derivates (acetoaminophen, salycilate and 5-aminosalycilate) as inhibitors of membrane lipid peroxidation and as peroxyl radical scavengers Arch. Biochem. Biophys. 1994, 315, 161-169
    • (1994) Arch. Biochem. Biophys. , vol.315 , pp. 161-169
    • Dinis, T.C.P.1    Madeira, V.M.C.2    Almeida, L.M.3
  • 32
    • 0003791868 scopus 로고
    • Ed. Academic Press: San Diego, CA
    • Ozols, J. D., Ed. Methods in Enzymology; Academic Press: San Diego, CA, 1990; Vol. 182.
    • (1990) Methods in Enzymology , vol.182
    • Ozols, J.D.1
  • 33
    • 0011650814 scopus 로고
    • Interfacial and emulsifying properties of whey peptides fraction obtained with a two step ultrafiltration process
    • Turgeon, S. L.; Gauthier, S. F.; Paquin, P. Interfacial and emulsifying properties of whey peptides fraction obtained with a two step ultrafiltration process J. Agric. Food Chem. 1991, 39 (4) 637-676
    • (1991) J. Agric. Food Chem. , vol.39 , Issue.4 , pp. 637-676
    • Turgeon, S.L.1    Gauthier, S.F.2    Paquin, P.3
  • 34
    • 69249206712 scopus 로고    scopus 로고
    • Antioxidant activity and functional properties of porcine plasma protein hydrolysate as influenced by the degree of hydrolysis
    • Liu, Q.; Kong, B.; Xiong, Y. L.; Xia, X. Antioxidant activity and functional properties of porcine plasma protein hydrolysate as influenced by the degree of hydrolysis Food Chem. 2010, 118, 403-410
    • (2010) Food Chem. , vol.118 , pp. 403-410
    • Liu, Q.1    Kong, B.2    Xiong, Y.L.3    Xia, X.4
  • 35
    • 29244443998 scopus 로고    scopus 로고
    • Antioxidant properties of ultrafiltration-recovered soy protein fractions from industrial effluents and their hydrolysates
    • Moure, A.; Domínguez, H.; Parajo, J. C. Antioxidant properties of ultrafiltration-recovered soy protein fractions from industrial effluents and their hydrolysates Process Biochem. (Oxford) 2006, 41, 447-456
    • (2006) Process Biochem. (Oxford) , vol.41 , pp. 447-456
    • Moure, A.1    Domínguez, H.2    Parajo, J.C.3
  • 36
    • 0034101865 scopus 로고    scopus 로고
    • Isolation and characterization of free radical scavenging activities peptides derived from casein
    • Suetsuna, K.; Ukeda, H.; Ochi, H. Isolation and characterization of free radical scavenging activities peptides derived from casein J. Nutr. Biochem. 2000, 11, 128-131
    • (2000) J. Nutr. Biochem. , vol.11 , pp. 128-131
    • Suetsuna, K.1    Ukeda, H.2    Ochi, H.3
  • 37
    • 34047153515 scopus 로고    scopus 로고
    • Purification and characterization of an antioxidant peptide obtained from tuna backbone protein by enzymatic hydrolysis
    • Je, J.-Y.; Qian, Z.-J.; Byun, H.-G.; Kim, S.-K. Purification and characterization of an antioxidant peptide obtained from tuna backbone protein by enzymatic hydrolysis Process Biochem. (Oxford) 2007, 42, 840-846
    • (2007) Process Biochem. (Oxford) , vol.42 , pp. 840-846
    • Je, J.-Y.1    Qian, Z.-J.2    Byun, H.-G.3    Kim, S.-K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.