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Volumn 15, Issue 10, 2017, Pages

Angiotensin I-converting enzyme (ACE) inhibitory activity, antioxidant properties, phenolic content and amino acid profiles of fucus spiralis L. Protein hydrolysate fractions

Author keywords

ACE inhibition; Amino acids composition; Antioxidant properties; Cardiovascular health; Edible brown algae; Marine functional foods; Peptide fractions; Phlorotannins; Protein enzymatic hydrolysate; Ultrafiltration

Indexed keywords

ALANINE; ALGAL EXTRACT; AMINO ACID; ANTIOXIDANT; ASPARTIC ACID; BROMELAIN; BUTYLCRESOL; CAPTOPRIL; DIPEPTIDYL CARBOXYPEPTIDASE; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; EDETIC ACID; FUCUS SPIRALIS EXTRACT; GLUTAMIC ACID; ISOLEUCINE; LEUCINE; LYSINE; METHIONINE; PHENOL DERIVATIVE; PHLOROGLUCINOL; PHLOROTANNIN; PROLINE; PROTEIN HYDROLYSATE; THREONINE; TYROSINE; UNCLASSIFIED DRUG; ANTIHYPERTENSIVE AGENT; SCAVENGER;

EID: 85032896933     PISSN: None     EISSN: 16603397     Source Type: Journal    
DOI: 10.3390/md15100311     Document Type: Article
Times cited : (76)

References (78)
  • 1
    • 79959736082 scopus 로고    scopus 로고
    • Marine bioactives as functional food ingredients: Potential to reduce the incidence of chronic diseases
    • Lordan, S.; Ross, R.P.; Stanton, C. Marine bioactives as functional food ingredients: Potential to reduce the incidence of chronic diseases. Mar. Drugs 2011, 9, 1056–1100. [PubMed]
    • (2011) Mar. Drugs , vol.9 , pp. 1056-1100
    • Lordan, S.1    Ross, R.P.2    Stanton, C.3
  • 2
    • 0035788194 scopus 로고    scopus 로고
    • Clinical effects of brown seaweed, Undaria pinnatifida (wakame), on blood pressure in hypertensive subjects
    • Hata, Y.; Nakajima, K.; Uchida, J.I.; Hidaka, H.; Nakano, T. Clinical effects of brown seaweed, Undaria pinnatifida (wakame), on blood pressure in hypertensive subjects. J. Clin. Biochem. Nutr. 2001, 30, 43–53. [CrossRef]
    • (2001) J. Clin. Biochem. Nutr. , vol.30 , pp. 43-53
    • Hata, Y.1    Nakajima, K.2    Uchida, J.I.3    Hidaka, H.4    Nakano, T.5
  • 3
    • 84978663462 scopus 로고    scopus 로고
    • Isolation and characterization of angiotensin I-converting enzyme (ACE) inhibitory peptides from Ulva rigida C. Agardh protein hydrolysate
    • Paiva, L.; Lima, E.; Neto, A.I.; Baptista, J. Isolation and characterization of angiotensin I-converting enzyme (ACE) inhibitory peptides from Ulva rigida C. Agardh protein hydrolysate. J. Funct. Foods 2016, 26, 65–76. [CrossRef]
    • (2016) J. Funct. Foods , vol.26 , pp. 65-76
    • Paiva, L.1    Lima, E.2    Neto, A.I.3    Baptista, J.4
  • 4
    • 0017102431 scopus 로고
    • Angiotensin-converting enzyme and the regulation of vasoactive peptides
    • Soffer, R.L. Angiotensin-converting enzyme and the regulation of vasoactive peptides. Annu. Rev. Biochem. 1976, 45, 73–94. [CrossRef] [PubMed]
    • (1976) Annu. Rev. Biochem. , vol.45 , pp. 73-94
    • Soffer, R.L.1
  • 5
    • 33644975021 scopus 로고    scopus 로고
    • Prehypertension, diabetes, and cardiovascular disease risk in a population-based sample: The strong heart study
    • Zhang, Y.; Lee, E.T.; Devereux, R.B.; Yeh, J.; Best, L.G.; Fabsitz, R.R.; Howard, B.V. Prehypertension, diabetes, and cardiovascular disease risk in a population-based sample: The strong heart study. Hypertension 2006, 47, 410–414. [CrossRef] [PubMed]
    • (2006) Hypertension , vol.47 , pp. 410-414
    • Zhang, Y.1    Lee, E.T.2    Devereux, R.B.3    Yeh, J.4    Best, L.G.5    Fabsitz, R.R.6    Howard, B.V.7
  • 6
    • 0021957042 scopus 로고
    • Conformational analysis and active site modelling of angiotensin-converting enzyme inhibitors
    • Andrews, P.R.; Carson, J.M.; Caselli, A.; Spark, M.J.; Woods, R. Conformational analysis and active site modelling of angiotensin-converting enzyme inhibitors. J. Med. Chem. 1985, 28, 393–399. [CrossRef] [PubMed]
    • (1985) J. Med. Chem. , vol.28 , pp. 393-399
    • Andrews, P.R.1    Carson, J.M.2    Caselli, A.3    Spark, M.J.4    Woods, R.5
  • 7
    • 0031769256 scopus 로고    scopus 로고
    • Purification and identification of angiotensin I-converting enzyme inhibitors from the red alga Porphyra yezoensis
    • Suetsuna, K. Purification and identification of angiotensin I-converting enzyme inhibitors from the red alga Porphyra yezoensis. J. Mar. Biotechnol. 1998, 6, 163–167. [PubMed]
    • (1998) J. Mar. Biotechnol. , vol.6 , pp. 163-167
    • Suetsuna, K.1
  • 8
    • 0037048736 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory peptides derived from Wakame (Undaria pinnatifida) and their antihypertensive effect in spontaneously hypertensive rats
    • Sato, M.; Hosokawa, T.; Yamaguchi, T.; Nakano, T.; Muramoto, K.; Kahara, T.; Funayama, K.; Kobayashi, A.; Nakano, T. Angiotensin I-converting enzyme inhibitory peptides derived from Wakame (Undaria pinnatifida) and their antihypertensive effect in spontaneously hypertensive rats. J. Agric. Food Chem. 2002, 50, 6245–6252. [CrossRef] [PubMed]
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 6245-6252
    • Sato, M.1    Hosokawa, T.2    Yamaguchi, T.3    Nakano, T.4    Muramoto, K.5    Kahara, T.6    Funayama, K.7    Kobayashi, A.8    Nakano, T.9
  • 9
    • 84991608470 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme (ACE) inhibitory activity of Fucus spiralis macroalgae and influence of the extracts storage temperature: A short report
    • Paiva, L.; Lima, E.; Neto, A.I.; Baptista, J. Angiotensin I-converting enzyme (ACE) inhibitory activity of Fucus spiralis macroalgae and influence of the extracts storage temperature: A short report. J. Pharm. Biomed. Anal. 2016, 131, 503–507. [CrossRef] [PubMed]
    • (2016) J. Pharm. Biomed. Anal. , vol.131 , pp. 503-507
    • Paiva, L.1    Lima, E.2    Neto, A.I.3    Baptista, J.4
  • 10
    • 33845580227 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme I inhibitory activity of phlorotannins from Ecklonia stolonifera
    • Jung, H.A.; Hyun, S.K.; Kim, H.R.; Choi, J.S. Angiotensin-converting enzyme I inhibitory activity of phlorotannins from Ecklonia stolonifera. Fish. Sci. 2006, 72, 1292–1299. [CrossRef]
    • (2006) Fish. Sci. , vol.72 , pp. 1292-1299
    • Jung, H.A.1    Hyun, S.K.2    Kim, H.R.3    Choi, J.S.4
  • 11
    • 77952564007 scopus 로고    scopus 로고
    • Angiotensin-I-converting enzyme (ACE) inhibitors from marine resources: Prospects in the pharmaceutical industry
    • Wijesekara, I.; Kim, S.-K. Angiotensin-I-converting enzyme (ACE) inhibitors from marine resources: Prospects in the pharmaceutical industry. Mar. Drugs 2010, 8, 1080–1093. [CrossRef] [PubMed]
    • (2010) Mar. Drugs , vol.8 , pp. 1080-1093
    • Wijesekara, I.1    Kim, S.-K.2
  • 12
    • 79956289369 scopus 로고    scopus 로고
    • Effect of phlorotannins isolated from Ecklonia cava on angiotensin I-converting enzyme (ACE) inhibitory activity
    • Wijesinghe, W.A.J.P.; Ko, S.-C.; Jeon, Y.-J. Effect of phlorotannins isolated from Ecklonia cava on angiotensin I-converting enzyme (ACE) inhibitory activity. Nutr. Res. Pract. 2011, 5, 93–100. [CrossRef] [PubMed]
    • (2011) Nutr. Res. Pract. , vol.5 , pp. 93-100
    • Wijesinghe, W.A.J.P.1    Ko, S.-C.2    Jeon, Y.-J.3
  • 13
    • 84961144505 scopus 로고    scopus 로고
    • Comparison of different extraction techniques for obtaining extracts from brown seaweeds and their potential effects as angiotensin I-converting enzyme (ACE) inhibitors
    • Olivares-Molina, A.; Fernández, K. Comparison of different extraction techniques for obtaining extracts from brown seaweeds and their potential effects as angiotensin I-converting enzyme (ACE) inhibitors. J. Appl. Phycol. 2016, 28, 1295–1302. [CrossRef]
    • (2016) J. Appl. Phycol. , vol.28 , pp. 1295-1302
    • Olivares-Molina, A.1    Fernández, K.2
  • 14
    • 85021130871 scopus 로고    scopus 로고
    • Fucaceae: A source of bioactive phlorotannins
    • Catarino, M.D.; Silva, A.M.S.; Cardoso, S.M. Fucaceae: A source of bioactive phlorotannins. Int. J. Mol. Sci. 2017, 18, 1327. [CrossRef] [PubMed]
    • (2017) Int. J. Mol. Sci. , vol.18 , pp. 1327
    • Catarino, M.D.1    Silva, A.M.S.2    Cardoso, S.M.3
  • 15
    • 79953294692 scopus 로고    scopus 로고
    • Bioactive proteins, peptides and amino acids from macroalgae
    • Harnedy, P.A.; FitzGerald, R.J. Bioactive proteins, peptides and amino acids from macroalgae. J. Phycol. 2011, 47, 218–232. [CrossRef] [PubMed]
    • (2011) J. Phycol. , vol.47 , pp. 218-232
    • Harnedy, P.A.1    FitzGerald, R.J.2
  • 16
    • 84866363079 scopus 로고    scopus 로고
    • Bio-functionalities of proteins derived from marine algae—A review
    • Samarakoon, K.; Jeon, Y.-J. Bio-functionalities of proteins derived from marine algae—A review. Food Res. Int. 2012, 48, 948–960. [CrossRef]
    • (2012) Food Res. Int. , vol.48 , pp. 948-960
    • Samarakoon, K.1    Jeon, Y.-J.2
  • 17
    • 84879994477 scopus 로고    scopus 로고
    • Enzyme proteolysis enhanced extraction of ACE inhibitory and antioxidant compounds (peptides and polyphenols) from Porphyra columbina residual cake
    • Cian, R.E.; Alaiz, M.; Vioque, J.; Drago, S.R. Enzyme proteolysis enhanced extraction of ACE inhibitory and antioxidant compounds (peptides and polyphenols) from Porphyra columbina residual cake. J. Appl. Phycol. 2013, 25, 1197–1206. [CrossRef]
    • (2013) J. Appl. Phycol. , vol.25 , pp. 1197-1206
    • Cian, R.E.1    Alaiz, M.2    Vioque, J.3    Drago, S.R.4
  • 18
    • 84928658905 scopus 로고    scopus 로고
    • Antioxidants: Characterization, natural sources, extraction and analysis
    • Oroian, M.; Escriche, I. Antioxidants: Characterization, natural sources, extraction and analysis. Food Res. Int. 2015, 74, 10–36. [CrossRef] [PubMed]
    • (2015) Food Res. Int. , vol.74 , pp. 10-36
    • Oroian, M.1    Escriche, I.2
  • 19
    • 0038397146 scopus 로고    scopus 로고
    • Food-derived bioactive peptides—Opportunities for designing future foods
    • Korhonen, H.; Pihlanto, A. Food-derived bioactive peptides—Opportunities for designing future foods. Curr. Pharm. Des. 2003, 9, 1297–1308. [CrossRef] [PubMed]
    • (2003) Curr. Pharm. Des. , vol.9 , pp. 1297-1308
    • Korhonen, H.1    Pihlanto, A.2
  • 20
    • 83055174569 scopus 로고    scopus 로고
    • Enzyme-assistant extraction (EAE) of bioactive components: A useful approach for recovery of industrially important metabolites from seaweeds: A review
    • Wijesinghe, W.A.; Jeon, Y.-J. Enzyme-assistant extraction (EAE) of bioactive components: A useful approach for recovery of industrially important metabolites from seaweeds: A review. Fitoterapia 2012, 83, 6–12. [CrossRef] [PubMed]
    • (2012) Fitoterapia , vol.83 , pp. 6-12
    • Wijesinghe, W.A.1    Jeon, Y.-J.2
  • 23
    • 84901946159 scopus 로고    scopus 로고
    • Edible Azorean macroalgae as source of rich nutrients with impact on human health
    • Paiva, L.; Lima, E.; Patarra, R.F.; Neto, A.I.; Baptista, J. Edible Azorean macroalgae as source of rich nutrients with impact on human health. Food Chem. 2014, 164, 128–135. [CrossRef] [PubMed]
    • (2014) Food Chem , vol.164 , pp. 128-135
    • Paiva, L.1    Lima, E.2    Patarra, R.F.3    Neto, A.I.4    Baptista, J.5
  • 24
    • 33748603467 scopus 로고    scopus 로고
    • Co-occurrence and antioxidant activities of fucol and fucophlorethol classes of polymeric phenols in Fucus spiralis
    • Cerantola, S.; Breton, F.; Ar Gall, E.; Deslandes, E. Co-occurrence and antioxidant activities of fucol and fucophlorethol classes of polymeric phenols in Fucus spiralis. Bot. Mar. 2006, 49, 347–351. [CrossRef]
    • (2006) Bot. Mar. , vol.49 , pp. 347-351
    • Cerantola, S.1    Breton, F.2    Ar Gall, E.3    Deslandes, E.4
  • 25
    • 84875950676 scopus 로고    scopus 로고
    • Enrichment of polyphenol contents and antioxidant activities of Irish brown macroalgae using food-friendly techniques based on polarity and molecular size
    • Tierney, M.S.; Smyth, T.J.; Rai, D.K.; Soler-Vila, A.; Croft, A.K.; Brunton, N. Enrichment of polyphenol contents and antioxidant activities of Irish brown macroalgae using food-friendly techniques based on polarity and molecular size. Food Chem. 2013, 139, 753–761. [CrossRef] [PubMed]
    • (2013) Food Chem , vol.139 , pp. 753-761
    • Tierney, M.S.1    Smyth, T.J.2    Rai, D.K.3    Soler-Vila, A.4    Croft, A.K.5    Brunton, N.6
  • 26
    • 84988643257 scopus 로고    scopus 로고
    • Cytoprotective effect of seaweeds with high antioxidant activity from the Peniche coast (Portugal)
    • Pinteus, S.; Silva, J.; Alves, C.; Horta, A.; Fino, N.; Inês Rodrigues, A.; Mendes, S.; Pedrosa, R. Cytoprotective effect of seaweeds with high antioxidant activity from the Peniche coast (Portugal). Food Chem. 2017, 218, 591–599. [CrossRef] [PubMed]
    • (2017) Food Chem , vol.218 , pp. 591-599
    • Pinteus, S.1    Silva, J.2    Alves, C.3    Horta, A.4    Fino, N.5    Inês Rodrigues, A.6    Mendes, S.7    Pedrosa, R.8
  • 27
    • 0032997695 scopus 로고    scopus 로고
    • Seaweed proteins: Biochemical nutritional aspects and potential uses
    • Fleurence, J. Seaweed proteins: Biochemical nutritional aspects and potential uses. Trends Food Sci. Technol. 1999, 10, 25–28. [CrossRef]
    • (1999) Trends Food Sci. Technol. , vol.10 , pp. 25-28
    • Fleurence, J.1
  • 29
    • 85032989882 scopus 로고    scopus 로고
    • Screening for angiotensin I-converting enzyme (ACE) inhibitory activity of enzymatic hydrolysates obtained from Azorean macroalgae
    • Paiva, L.; Lima, E.; Neto, A.I.; Baptista, J. Screening for angiotensin I-converting enzyme (ACE) inhibitory activity of enzymatic hydrolysates obtained from Azorean macroalgae. Arquipél. Life Mar. Sci. 2015, 32, 11–17.
    • (2015) Arquipél. Life Mar. Sci. , vol.32 , pp. 11-17
    • Paiva, L.1    Lima, E.2    Neto, A.I.3    Baptista, J.4
  • 30
    • 84902361374 scopus 로고    scopus 로고
    • Antioxidant and functional properties of fish protein hydrolysates from fresh water carp (Catla catla) as influenced by the nature of enzyme
    • Elavarasan, K.; Kumar, V.N.; Shamasundar, B.A. Antioxidant and functional properties of fish protein hydrolysates from fresh water carp (Catla catla) as influenced by the nature of enzyme. J. Food Process. Preserv. 2014, 38, 1207–1214. [CrossRef]
    • (2014) J. Food Process. Preserv. , vol.38 , pp. 1207-1214
    • Elavarasan, K.1    Kumar, V.N.2    Shamasundar, B.A.3
  • 31
    • 84988698596 scopus 로고    scopus 로고
    • Bioactive and functional properties of protein hydrolysates from fish frame processing waste using plant proteases
    • Gajanan, P.G.; Elavarasan, K.; Shamasundar, B.A. Bioactive and functional properties of protein hydrolysates from fish frame processing waste using plant proteases. Environ. Sci. Pollut. Res. 2016, 23, 24901–24911. [CrossRef] [PubMed]
    • (2016) Environ. Sci. Pollut. Res. , vol.23 , pp. 24901-24911
    • Gajanan, P.G.1    Elavarasan, K.2    Shamasundar, B.A.3
  • 32
    • 85018640215 scopus 로고    scopus 로고
    • Optimization of bromelain-aided production of angiotensin I-converting enzyme inhibitory hydrolysates from stone fish using response surface methodology
    • Auwal, S.M.; Zarei, M.; Abdul-Hamid, A.; Saari, N. Optimization of bromelain-aided production of angiotensin I-converting enzyme inhibitory hydrolysates from stone fish using response surface methodology. Mar. Drugs 2017, 15, 104. [CrossRef] [PubMed]
    • (2017) Mar. Drugs , vol.15 , pp. 104
    • Auwal, S.M.1    Zarei, M.2    Abdul-Hamid, A.3    Saari, N.4
  • 33
    • 84908702221 scopus 로고    scopus 로고
    • ACE inhibitory, hypotensive and antioxidant peptide fractions from Mucuna pruriens proteins
    • Chalé, F.G.H.; Ruiz, J.C.R.; Fernández, J.J.A.; Ancona, D.A.B.; Campos, M.R.S. ACE inhibitory, hypotensive and antioxidant peptide fractions from Mucuna pruriens proteins. Process Biochem. 2014, 49, 1691–1698. [CrossRef]
    • (2014) Process Biochem. , vol.49 , pp. 1691-1698
    • Chalé, F.G.H.1    Ruiz, J.C.R.2    Fernández, J.J.A.3    Ancona, D.A.B.4    Campos, M.R.S.5
  • 34
    • 79957795842 scopus 로고    scopus 로고
    • Chemometric analysis of the amino acid requirements of antioxidant food protein hydrolysates
    • Udenigwe, C.C.; Aluko, R.E. Chemometric analysis of the amino acid requirements of antioxidant food protein hydrolysates. Int. J. Mol. Sci. 2011, 12, 3148–3161. [CrossRef] [PubMed]
    • (2011) Int. J. Mol. Sci. , vol.12 , pp. 3148-3161
    • Udenigwe, C.C.1    Aluko, R.E.2
  • 35
    • 40049102915 scopus 로고    scopus 로고
    • Seaweed proteins
    • Yada, R.Y., Ed.; Woodhead Publishing Limited: Cambridge, UK
    • Fleurence, J. Seaweed proteins. In Proteins in Food Processing; Yada, R.Y., Ed.; Woodhead Publishing Limited: Cambridge, UK, 2004; pp. 197–213.
    • (2004) Proteins in Food Processing , pp. 197-213
    • Fleurence, J.1
  • 36
    • 30944462286 scopus 로고    scopus 로고
    • Study and development of a defatted wheat germ nutritive noodle
    • Ge, Y.; Sun, A.; Ni, Y.; Cai, T. Study and development of a defatted wheat germ nutritive noodle. Eur. Food Res. Technol. 2001, 212, 344–348. [CrossRef]
    • (2001) Eur. Food Res. Technol. , vol.212 , pp. 344-348
    • Ge, Y.1    Sun, A.2    Ni, Y.3    Cai, T.4
  • 37
    • 33744948606 scopus 로고    scopus 로고
    • Screening for angiotensin I-converting enzyme inhibitory activity of Ecklonia cava
    • Athukorala, Y.; Jeon, Y.J. Screening for angiotensin I-converting enzyme inhibitory activity of Ecklonia cava. J. Food Sci. Nutr. 2005, 10, 134–139. [CrossRef]
    • (2005) J. Food Sci. Nutr. , vol.10 , pp. 134-139
    • Athukorala, Y.1    Jeon, Y.J.2
  • 38
    • 84921691991 scopus 로고    scopus 로고
    • Antioxidant activity of the brown macroalgae Fucus spiralis Linnaeus harvested from the west coast of Ireland
    • Tierney, M.S.; Soler-vila, A.; Croft, A.K.; Hayes, M. Antioxidant activity of the brown macroalgae Fucus spiralis Linnaeus harvested from the west coast of Ireland. Curr. Res. J. Biol. Sci. 2013, 5, 81–90.
    • (2013) Curr. Res. J. Biol. Sci. , vol.5 , pp. 81-90
    • Tierney, M.S.1    Soler-Vila, A.2    Croft, A.K.3    Hayes, M.4
  • 41
    • 84871755028 scopus 로고    scopus 로고
    • Phlorotannin extracts from Fucales characterized by HPLC-DAD-ESI-MSn: Approaches to hyaluronidase inhibitory capacity and antioxidant properties
    • Ferreres, F.; Lopes, G.; Gil-Izquierdo, A.; Andrade, P.B.; Sousa, C.; Mouga, T.; Valentão, P. Phlorotannin extracts from Fucales characterized by HPLC-DAD-ESI-MSn: Approaches to hyaluronidase inhibitory capacity and antioxidant properties. Mar. Drugs 2012, 10, 2766–2781. [CrossRef] [PubMed]
    • (2012) Mar. Drugs , vol.10 , pp. 2766-2781
    • Ferreres, F.1    Lopes, G.2    Gil-Izquierdo, A.3    Andrade, P.B.4    Sousa, C.5    Mouga, T.6    Valentão, P.7
  • 42
    • 67349231325 scopus 로고    scopus 로고
    • A novel ACE inhibitory peptide isolated from Acaudina molpadioidea hydrolysate
    • Zhao, Y.; Li, B.; Dong, S.; Liu, Z.; Zhao, X.; Wang, J.; Zeng, M. A novel ACE inhibitory peptide isolated from Acaudina molpadioidea hydrolysate. Peptides 2009, 30, 1028–1033. [CrossRef] [PubMed]
    • (2009) Peptides , vol.30 , pp. 1028-1033
    • Zhao, Y.1    Li, B.2    Dong, S.3    Liu, Z.4    Zhao, X.5    Wang, J.6    Zeng, M.7
  • 43
    • 24944554968 scopus 로고    scopus 로고
    • Mung-bean protein hydrolysates obtained with Alcalase exhibit angiotensin I-converting enzyme inhibitory activity
    • Hong, L.G.; Wei, L.G.; Liu, H.; Hui, S.Y. Mung-bean protein hydrolysates obtained with Alcalase exhibit angiotensin I-converting enzyme inhibitory activity. Food Sci. Technol. Int. 2005, 11, 281–287.
    • (2005) Food Sci. Technol. Int. , vol.11 , pp. 281-287
    • Hong, L.G.1    Wei, L.G.2    Liu, H.3    Hui, S.Y.4
  • 44
    • 79959969840 scopus 로고    scopus 로고
    • Angiotensin-I-converting enzyme and prolyl endopeptidase inhibitory peptides from natural sources with a focus on marine processing by-products
    • Wilson, J.; Hayes, M.; Carney, B. Angiotensin-I-converting enzyme and prolyl endopeptidase inhibitory peptides from natural sources with a focus on marine processing by-products. Food Chem. 2011, 129, 235–244. [CrossRef]
    • (2011) Food Chem , vol.129 , pp. 235-244
    • Wilson, J.1    Hayes, M.2    Carney, B.3
  • 46
    • 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. Int. J. Mol. Sci. 2015, 16, 28870–28885. [CrossRef] [PubMed]
    • (2015) Int. J. Mol. Sci. , vol.16 , pp. 28870-28885
    • Ghanbari, R.1    Zarei, M.2    Ebrahimpour, A.3    Abdul-Hamid, A.4    Ismail, A.5    Saari, N.6
  • 47
    • 0037627830 scopus 로고    scopus 로고
    • Antihypertensive effects of tannins isolated from traditional Chinese herbs as non-specific inhibitors of angiotensin converting enzyme
    • Liu, J.-C.; Hsu, F.-L.; Tsai, J.-C.; Chan, P.; Liu, J.Y.; Thomas, G.N.; Tomlinson, B.; Lo, M.-Y.; Lin, J.-Y. Antihypertensive effects of tannins isolated from traditional Chinese herbs as non-specific inhibitors of angiotensin converting enzyme. Life Sci. 2003, 73, 1543–1555. [CrossRef]
    • (2003) Life Sci. , vol.73 , pp. 1543-1555
    • Liu, J.-C.1    Hsu, F.-L.2    Tsai, J.-C.3    Chan, P.4    Liu, J.Y.5    Thomas, G.N.6    Tomlinson, B.7    Lo, M.-Y.8    Lin, J.-Y.9
  • 49
    • 84870217899 scopus 로고    scopus 로고
    • Purification and identification of antioxidant peptides from enzymatic hydrolysates of Tilapia (Oreochromis niloticus) frame protein
    • Fan, J.; He, J.; Zhuang, Y.; Sun, L. Purification and identification of antioxidant peptides from enzymatic hydrolysates of Tilapia (Oreochromis niloticus) frame protein. Molecules 2012, 17, 12836–12850. [CrossRef] [PubMed]
    • (2012) Molecules , vol.17 , pp. 12836-12850
    • Fan, J.1    He, J.2    Zhuang, Y.3    Sun, L.4
  • 50
    • 64549113397 scopus 로고    scopus 로고
    • Flaxseed protein-derived peptide fractions: Antioxidant properties and inhibition of lipopolysaccharide-induced nitric oxide production in murine macrophages
    • Udenigwe, C.C.; Lu, Y.-L.; Han, C.-H.; Hou, W.-C.; Aluko, R.E. Flaxseed protein-derived peptide fractions: Antioxidant properties and inhibition of lipopolysaccharide-induced nitric oxide production in murine macrophages. Food Chem. 2009, 116, 277–284. [CrossRef]
    • (2009) Food Chem , vol.116 , pp. 277-284
    • Udenigwe, C.C.1    Lu, Y.-L.2    Han, C.-H.3    Hou, W.-C.4    Aluko, R.E.5
  • 51
    • 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.; Nokihara, K. Antioxidative properties of histidine-containing peptides designed from peptide fragments found in the digests of a soybean protein. J. Agric. Food. Chem. 1998, 46, 49–53. [CrossRef] [PubMed]
    • (1998) J. Agric. Food. Chem. , vol.46 , pp. 49-53
    • Chen, H.-M.1    Muramoto, K.2    Yamauchi, F.3    Fujimoto, K.4    Nokihara, K.5
  • 52
    • 52949145637 scopus 로고    scopus 로고
    • Structures and properties of antioxidative peptides derived from royal jelly protein
    • Guo, H.; Kouzuma, Y.; Yonekura, M. Structures and properties of antioxidative peptides derived from royal jelly protein. Food Chem. 2009, 113, 238–245. [CrossRef]
    • (2009) Food Chem. , vol.113 , pp. 238-245
    • Guo, H.1    Kouzuma, Y.2    Yonekura, M.3
  • 53
    • 11144293558 scopus 로고    scopus 로고
    • Purification of a radical scavenging peptide from fermented mussel sauce and its antioxidant properties
    • Rajapakse, N.; Mendis, E.; Jung, W.-K.; Je, J.-Y.; Kim, S.-K. Purification of a radical scavenging peptide from fermented mussel sauce and its antioxidant properties. Food. Res. Int. 2005, 38, 175–182. [CrossRef]
    • (2005) Food. Res. Int. , vol.38 , pp. 175-182
    • Rajapakse, N.1    Mendis, E.2    Jung, W.-K.3    Je, J.-Y.4    Kim, S.-K.5
  • 54
    • 84929208726 scopus 로고    scopus 로고
    • Purification and characterization of antioxidant peptides from enzymatically hydrolyzed chicken egg white
    • Nimalaratne, C.; Bandara, N.; Wu, J. Purification and characterization of antioxidant peptides from enzymatically hydrolyzed chicken egg white. Food Chem. 2015, 188, 467–472. [CrossRef] [PubMed]
    • (2015) Food Chem , vol.188 , pp. 467-472
    • Nimalaratne, C.1    Bandara, N.2    Wu, J.3
  • 56
    • 84897355063 scopus 로고    scopus 로고
    • Phenolic content and antioxidant activity of fractions obtained from selected Irish macroalgae species (Laminaria digitata, Fucus serratus, Gracilaria gracilis and Codium fragile)
    • Heffernan, N.; Smyth, T.J.; Soler-Villa, A.; Fitzgerald, R.J.; Brunton, N.P. Phenolic content and antioxidant activity of fractions obtained from selected Irish macroalgae species (Laminaria digitata, Fucus serratus, Gracilaria gracilis and Codium fragile). J. Appl. Phycol. 2015, 27, 519–530. [CrossRef]
    • (2015) J. Appl. Phycol. , vol.27 , pp. 519-530
    • Heffernan, N.1    Smyth, T.J.2    Soler-Villa, A.3    Fitzgerald, R.J.4    Brunton, N.P.5
  • 57
    • 33750180924 scopus 로고    scopus 로고
    • Protective effect of Ecklonia cava enzymatic extracts on hydrogen peroxide-induced cell damage
    • Kim, K.N.; Heo, S.-J.; Song, C.B.; Lee, J.; Heo, M.S.; Yeo, I.K.; Kang, K.; Hyun, J.W.; Jeon, Y.-J. Protective effect of Ecklonia cava enzymatic extracts on hydrogen peroxide-induced cell damage. Process Biochem. 2006, 41, 2393–2401. [CrossRef]
    • (2006) Process Biochem. , vol.41 , pp. 2393-2401
    • Kim, K.N.1    Heo, S.-J.2    Song, C.B.3    Lee, J.4    Heo, M.S.5    Yeo, I.K.6    Kang, K.7    Hyun, J.W.8    Jeon, Y.-J.9
  • 58
    • 64649096209 scopus 로고    scopus 로고
    • Total phenolic compounds, radical scavenging and metal chelation of extracts from Icelandic seaweeds
    • Wang, T.; Jónsdóttir, R.; Ólafsdóttir, G. Total phenolic compounds, radical scavenging and metal chelation of extracts from Icelandic seaweeds. Food Chem. 2009, 116, 240–248. [CrossRef]
    • (2009) Food Chem , vol.116 , pp. 240-248
    • Wang, T.1    Jónsdóttir, R.2    Ólafsdóttir, G.3
  • 59
    • 79959948783 scopus 로고    scopus 로고
    • Affinity purification and characterisation of chelating peptides from chickpea protein hydrolysates
    • Torres-Fuentes, C.; Alaiz, M.; Vioque, J. Affinity purification and characterisation of chelating peptides from chickpea protein hydrolysates. Food Chem. 2011, 129, 485–490. [CrossRef]
    • (2011) Food Chem , vol.129 , pp. 485-490
    • Torres-Fuentes, C.1    Alaiz, M.2    Vioque, J.3
  • 60
    • 79953044211 scopus 로고    scopus 로고
    • In vitro antioxidant properties of hemp seed (Cannabis sativa L.) protein hydrolysate fractions
    • Girgih, A.T.; Udenigwe, C.C.; Aluko, R.E. In vitro antioxidant properties of hemp seed (Cannabis sativa L.) protein hydrolysate fractions. J. Am. Oil Chem. Soc. 2011, 88, 381–389. [CrossRef]
    • (2011) J. Am. Oil Chem. Soc. , vol.88 , pp. 381-389
    • Girgih, A.T.1    Udenigwe, C.C.2    Aluko, R.E.3
  • 61
    • 33645728386 scopus 로고    scopus 로고
    • Antioxidant potential of Ecklonia cava on reactive oxygen species scavenging, metal chelating, reducing power and lipid peroxidation inhibition
    • Senevirathne, M.; Kim, S.-H.; Siriwardhana, N.; Ha, J.-H.; Lee, K.-W.; Jeon, Y.-J. Antioxidant potential of Ecklonia cava on reactive oxygen species scavenging, metal chelating, reducing power and lipid peroxidation inhibition. Rev. Agaroquim. Tecnol. Aliment. 2006, 12, 27–38.
    • (2006) Rev. Agaroquim. Tecnol. Aliment. , vol.12 , pp. 27-38
    • Senevirathne, M.1    Kim, S.-H.2    Siriwardhana, N.3    Ha, J.-H.4    Lee, K.-W.5    Jeon, Y.-J.6
  • 62
    • 1542381085 scopus 로고    scopus 로고
    • Anti-oxidant activity of methanol extracts from Indonesian seaweeds in an oil emulsion model
    • Santoso, J.; Yoshie-Stark, Y.; Suzuki, T. Anti-oxidant activity of methanol extracts from Indonesian seaweeds in an oil emulsion model. Fish. Sci. 2004, 70, 183–188. [CrossRef]
    • (2004) Fish. Sci. , vol.70 , pp. 183-188
    • Santoso, J.1    Yoshie-Stark, Y.2    Suzuki, T.3
  • 63
    • 0032046437 scopus 로고    scopus 로고
    • Antioxidant activity of burdock (Arctium lappa Linné): It’s scavenging effect on free radical and active oxygen
    • Duh, P.-D. Antioxidant activity of burdock (Arctium lappa Linné): It’s scavenging effect on free radical and active oxygen. J. Am. Oil Chem. Soc. 1998, 75, 455–461. [CrossRef]
    • (1998) J. Am. Oil Chem. Soc. , vol.75 , pp. 455-461
    • Duh, P.-D.1
  • 64
    • 36148983029 scopus 로고    scopus 로고
    • In vitro antioxidant activities of three selected brown seaweeds of India
    • Chandini, S.-K.; Ganesan, P.; Bhaskar, N. In vitro antioxidant activities of three selected brown seaweeds of India. Food Chem. 2008, 107, 707–713. [CrossRef]
    • (2008) Food Chem , vol.107 , pp. 707-713
    • Chandini, S.-K.1    Ganesan, P.2    Bhaskar, N.3
  • 65
    • 38849200525 scopus 로고    scopus 로고
    • Antioxidant properties of methanol extract and its solvent fractions obtained from selected Indian red seaweeds
    • Ganesan, P.; Kumar, C.S.; Bhaskar, N. Antioxidant properties of methanol extract and its solvent fractions obtained from selected Indian red seaweeds. Bioresour. Technol. 2008, 99, 2717–2723. [CrossRef] [PubMed]
    • (2008) Bioresour. Technol. , vol.99 , pp. 2717-2723
    • Ganesan, P.1    Kumar, C.S.2    Bhaskar, N.3
  • 67
    • 79955086761 scopus 로고    scopus 로고
    • Bio-prospecting of a few brown seaweeds for their cytotoxic and antioxidant activities
    • Vinayak, R.C.; Sabu, A.S.; Chatterji, A. Bio-prospecting of a few brown seaweeds for their cytotoxic and antioxidant activities. Evid. Based Complement. Altern. Med. 2011. [CrossRef] [PubMed]
    • (2011) Evid. Based Complement. Altern. Med
    • Vinayak, R.C.1    Sabu, A.S.2    Chatterji, A.3
  • 68
    • 78651436134 scopus 로고    scopus 로고
    • Total phenolic content and antioxidant capacity of extracts obtained from six important fruit residues
    • Babbar, N.; Oberoi, H.S.; Uppal, D.S.; Patil, R.T. Total phenolic content and antioxidant capacity of extracts obtained from six important fruit residues. Food Res. Int. 2011, 44, 391–396. [CrossRef]
    • (2011) Food Res. Int. , vol.44 , pp. 391-396
    • Babbar, N.1    Oberoi, H.S.2    Uppal, D.S.3    Patil, R.T.4
  • 69
    • 77949311512 scopus 로고    scopus 로고
    • Phytochelatins: Peptides involved in heavy metal detoxification
    • Pal, R.; Rai, J.P. Phytochelatins: Peptides involved in heavy metal detoxification. Appl. Biochem. Biotechnol. 2010, 160, 945–963. [CrossRef] [PubMed]
    • (2010) Appl. Biochem. Biotechnol. , vol.160 , pp. 945-963
    • Pal, R.1    Rai, J.P.2
  • 70
    • 1842533485 scopus 로고    scopus 로고
    • Nutritional evaluation of protein concentrates isolated from two red seaweeds: Hypnea charoides and Hypnea japonica in growing rats
    • Wong, K.H.; Cheung, P.C.K.; Ang, P.O., Jr. Nutritional evaluation of protein concentrates isolated from two red seaweeds: Hypnea charoides and Hypnea japonica in growing rats. Hydrobiologia 2004, 512, 271–278. [CrossRef]
    • (2004) Hydrobiologia , vol.512 , pp. 271-278
    • Wong, K.H.1    Cheung, P.C.K.2    Ang, P.O.3
  • 71
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248–254. [CrossRef]
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 72
    • 85023595477 scopus 로고    scopus 로고
    • Nutritional and functional bioactivity value of selected Azorean macroalgae: Ulva compressa, Ulva rigida, Gelidium microdon, and Pterocladiella capillacea
    • Paiva, L.; Lima, E.; Neto, A.I.; Massimo, M.; Baptista, J. Nutritional and functional bioactivity value of selected Azorean macroalgae: Ulva compressa, Ulva rigida, Gelidium microdon, and Pterocladiella capillacea. J. Food Sci. 2017, 82, 1757–1764. [CrossRef] [PubMed]
    • (2017) J. Food Sci. , vol.82 , pp. 1757-1764
    • Paiva, L.1    Lima, E.2    Neto, A.I.3    Massimo, M.4    Baptista, J.5
  • 73
    • 85022241054 scopus 로고
    • Spectrophotometric assay using O-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins
    • Church, F.C.; Swaisgood, H.E.; Porter, D.H.; Catignani, G.L. Spectrophotometric assay using O-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins. J. Dairy Sci. 1983, 66, 1219–1227. [CrossRef]
    • (1983) J. Dairy Sci. , vol.66 , pp. 1219-1227
    • Church, F.C.1    Swaisgood, H.E.2    Porter, D.H.3    Catignani, G.L.4
  • 74
    • 1942428024 scopus 로고    scopus 로고
    • Determination of total phenolics
    • Wrolstad, R.E., Ed.; John Wiley & Sons: New York, NY, USA
    • Waterhouse, A.L. Determination of total phenolics. In Current Protocols in Food Analytical Chemistry; Wrolstad, R.E., Ed.; John Wiley & Sons: New York, NY, USA, 2002.
    • (2002) Current Protocols in Food Analytical Chemistry
    • Waterhouse, A.L.1
  • 75
    • 0015083353 scopus 로고
    • Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung
    • Cushman, D.W.; Cheung, H.S. Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung. Biochem. Pharmacol. 1971, 20, 1637–1648. [CrossRef]
    • (1971) Biochem. Pharmacol. , vol.20 , pp. 1637-1648
    • Cushman, D.W.1    Cheung, H.S.2
  • 76
    • 14644409019 scopus 로고    scopus 로고
    • The use of the stable free radical diphenylpicrylhydrazyl (DPPH) for estimating antioxidant activity
    • Molyneux, P. The use of the stable free radical diphenylpicrylhydrazyl (DPPH) for estimating antioxidant activity. Songklanakarin J. Sci. Technol. 2004, 26, 211–219.
    • (2004) Songklanakarin J. Sci. Technol. , vol.26 , pp. 211-219
    • Molyneux, P.1
  • 77
    • 80051869614 scopus 로고    scopus 로고
    • Antioxidant, antihypertensive and antimicrobial properties of ovine milk caseinate hydrolyzed with a microbial protease
    • Corrêa, A.P.; Daroit, D.J.; Coelho, J.; Meira, S.M.; Lopes, F.C.; Risso, P.H.; Brandelli, A. Antioxidant, antihypertensive and antimicrobial properties of ovine milk caseinate hydrolyzed with a microbial protease. J. Sci. Food Agric. 2011, 91, 2247–2254. [CrossRef] [PubMed]
    • (2011) J. Sci. Food Agric. , vol.91 , pp. 2247-2254
    • Corrêa, A.P.1    Daroit, D.J.2    Coelho, J.3    Meira, S.M.4    Lopes, F.C.5    Risso, P.H.6    Brandelli, A.7
  • 78
    • 0000209774 scopus 로고
    • Studies on products of browning reactions: Antioxidative activities of products of browning reaction prepared from glucosamine
    • Oyaizu, M. Studies on products of browning reactions: Antioxidative activities of products of browning reaction prepared from glucosamine. Jpn. J. Nutr. 1986, 44, 307–315. [CrossRef]
    • (1986) Jpn. J. Nutr. , vol.44 , pp. 307-315
    • Oyaizu, M.1


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