메뉴 건너뛰기




Volumn 229, Issue 6, 2009, Pages 915-921

Effects of heat treatment and in vitro digestion on the angiotensin converting enzyme inhibitory activity of some legume species

Author keywords

Ace inhibitory activity; Common dry beans; Dry pinto beans; Green lentils; Heat treatment; In vitro digestion

Indexed keywords

ACE-INHIBITORY ACTIVITY; DRY BEANS; DRY PINTO BEANS; IN-VITRO; PINTO BEANS;

EID: 77952098905     PISSN: 14382377     EISSN: 14382385     Source Type: Journal    
DOI: 10.1007/s00217-009-1133-x     Document Type: Article
Times cited : (84)

References (37)
  • 1
    • 34147123803 scopus 로고    scopus 로고
    • Food-derived peptides with biological activity: From research to food applications
    • Hartmann R, Meisel H (2007) Food-derived peptides with biological activity: from research to food applications. Curr Opin Biotech 18:163-169
    • (2007) Curr Opin Biotech , vol.18 , pp. 163-169
    • Hartmann, R.1    Meisel, H.2
  • 2
    • 0001586967 scopus 로고    scopus 로고
    • Biochemical properties of bioactive peptides derived from milk proteins: Potential nutraceuticals for food and pharmaceutical applications
    • Meisel H (1997) Biochemical properties of bioactive peptides derived from milk proteins: potential nutraceuticals for food and pharmaceutical applications. Livest Prod Sci 50:125-138
    • (1997) Livest Prod Sci , vol.50 , pp. 125-138
    • Meisel, H.1
  • 3
    • 33747503962 scopus 로고    scopus 로고
    • Bioactive peptides: Production and functionality
    • Korhonen H, Pihlanto A (2006) Bioactive peptides: production and functionality. Int Dairy J 16:945-960
    • (2006) Int Dairy J , vol.16 , pp. 945-960
    • Korhonen, H.1    Pihlanto, A.2
  • 4
    • 3242774456 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects
    • Li G-H, Le G-W, Shi Y-H, Shrestha S (2004) Angiotensin I-converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects. Nutr Res 24:469-486
    • (2004) Nutr Res , vol.24 , pp. 469-486
    • Li, G.-H.1    Le, G.-W.2    Shi, Y.-H.3    Shrestha, S.4
  • 5
    • 51049097278 scopus 로고    scopus 로고
    • The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease
    • Erdmann K, Cheung BWY, Schroder H (2008) The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease. J Nutr Biochem 19:643-654
    • (2008) J Nutr Biochem , vol.19 , pp. 643-654
    • Erdmann, K.1    Cheung, B.W.Y.2    Schroder, H.3
  • 6
    • 2342569607 scopus 로고    scopus 로고
    • A quantitative in silico analysis calculates the angiotensin I converting enzyme (ACE) inhibitory activity in pea and whey protein digests
    • Vermeirssen V, van der Bent A, Van Camp J, van Amerongen A, Verstraete W (2004) A quantitative in silico analysis calculates the angiotensin I converting enzyme (ACE) inhibitory activity in pea and whey protein digests. Biochimie 86:231-239
    • (2004) Biochimie , vol.86 , pp. 231-239
    • Vermeirssen, V.1    van der Bent, A.2    van Camp, J.3    van Amerongen, A.4    Verstraete, W.5
  • 7
    • 0037409169 scopus 로고    scopus 로고
    • Production of ace inhibitory peptides by digestion of chickpea legumin with alcalase
    • Yust MM, Pedroche J, Girón-Calle J, Alaiz M, Millán F, Vioque J (2003) Production of ace inhibitory peptides by digestion of chickpea legumin with alcalase. Food Chem 81:363-369
    • (2003) Food Chem , vol.81 , pp. 363-369
    • Yust, M.M.1    Pedroche, J.2    Girón-Calle, J.3    Alaiz, M.4    Millán, F.5    Vioque, J.6
  • 8
    • 0034951098 scopus 로고    scopus 로고
    • Purification and characterization of angiotensin I converting enzyme (ACE) inhibitory peptides from Alaska pollack (Theragra chalcogramma) skin
    • Byun H-G, Kim S-K (2001) Purification and characterization of angiotensin I converting enzyme (ACE) inhibitory peptides from Alaska pollack (Theragra chalcogramma) skin. Process Biochem 36:1155-1162
    • (2001) Process Biochem , vol.36 , pp. 1155-1162
    • Byun, H.-G.1    Kim, S.-K.2
  • 9
    • 0036868054 scopus 로고    scopus 로고
    • Hypotensive activity of muscle protein and gluten hydrolysates obtained by protease treatment
    • Saiga A, Kanda K, Wei Z, Okumura T, Kaneko T, Nishimura T (2002) Hypotensive activity of muscle protein and gluten hydrolysates obtained by protease treatment. J Food Biochem 26:391-401
    • (2002) J Food Biochem , vol.26 , pp. 391-401
    • Saiga, A.1    Kanda, K.2    Wei, Z.3    Okumura, T.4    Kaneko, T.5    Nishimura, T.6
  • 10
    • 34548321815 scopus 로고    scopus 로고
    • Angiotensin converting enzyme inhibition of fish protein hydrolysates prepared from alkaline-aided channel catfish protein isolate
    • Theodore AE, Kristinsson HG (2007) Angiotensin converting enzyme inhibition of fish protein hydrolysates prepared from alkaline-aided channel catfish protein isolate. J Sci Food Agric 87:2353-2357
    • (2007) J Sci Food Agric , vol.87 , pp. 2353-2357
    • Theodore, A.E.1    Kristinsson, H.G.2
  • 11
    • 0031464182 scopus 로고    scopus 로고
    • Angiotensin-I-converting enzyme inhibitory activities of gastric and pancreatic proteinase digests of whey proteins
    • Mullally MM, Meisel H, FitzGerald RJ (1997) Angiotensin-I-converting enzyme inhibitory activities of gastric and pancreatic proteinase digests of whey proteins. Int Dairy J 7:299-303
    • (1997) Int Dairy J , vol.7 , pp. 299-303
    • Mullally, M.M.1    Meisel, H.2    Fitzgerald, R.J.3
  • 12
    • 34047274420 scopus 로고    scopus 로고
    • Quantification of the angiotensin-converting enzyme-inhibiting tripeptides Val-Pro-Pro and Ile-Pro-Pro in hard, semi-hard and soft cheeses
    • Butikofer U, Meyer J, Sieber R, Wechsler D (2007) Quantification of the angiotensin-converting enzyme-inhibiting tripeptides Val-Pro-Pro and Ile-Pro-Pro in hard, semi-hard and soft cheeses. Int Dairy J 17:968-975
    • (2007) Int Dairy J , vol.17 , pp. 968-975
    • Butikofer, U.1    Meyer, J.2    Sieber, R.3    Wechsler, D.4
  • 13
    • 57149088481 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory peptides in skim milk fermented with Lactobacillus helveticus 130B4 from camel milk in Inner Mongolia, China
    • Quan S, Tsuda H, Miyamoto T (2008) Angiotensin I-converting enzyme inhibitory peptides in skim milk fermented with Lactobacillus helveticus 130B4 from camel milk in Inner Mongolia, China. J Sci Food Agric 88:2688-2692
    • (2008) J Sci Food Agric , vol.88 , pp. 2688-2692
    • Quan, S.1    Tsuda, H.2    Miyamoto, T.3
  • 14
    • 34147167071 scopus 로고    scopus 로고
    • Antihypertensive, ACE-inhibitory and vasodilator properties of an egg white hydrolysate: Effect of a simulated intestinal digestion
    • Miguel M, Alonso MJ, Salaices M, Aleixandre A, López-Fandiño R (2007) Antihypertensive, ACE-inhibitory and vasodilator properties of an egg white hydrolysate: effect of a simulated intestinal digestion. Food Chem 104:163-168
    • (2007) Food Chem , vol.104 , pp. 163-168
    • Miguel, M.1    Alonso, M.J.2    Salaices, M.3    Aleixandre, A.4    López-Fandiño, R.5
  • 15
    • 0037679233 scopus 로고    scopus 로고
    • Preparation of angiotensin I converting enzyme inhibitor from corn gluten
    • Suh HJ, Whang JH, Kim YS, Bae SH, Noh DO (2003) Preparation of angiotensin I converting enzyme inhibitor from corn gluten. Process Biochem 38:1239-1244
    • (2003) Process Biochem , vol.38 , pp. 1239-1244
    • Suh, H.J.1    Whang, J.H.2    Kim, Y.S.3    Bae, S.H.4    Noh, D.O.5
  • 16
    • 21244482606 scopus 로고    scopus 로고
    • Enhancement of angiotensin I converting enzyme inhibitory activity and improvement of the emulsifying and foaming properties of corn gluten hydrolysate using ultrafiltration membranes
    • Kim JM, Whang JH, Suh HJ (2004) Enhancement of angiotensin I converting enzyme inhibitory activity and improvement of the emulsifying and foaming properties of corn gluten hydrolysate using ultrafiltration membranes. Eur Food Res Technol 218: 133-138
    • (2004) Eur Food Res Technol , vol.218 , pp. 133-138
    • Kim, J.M.1    Whang, J.H.2    Suh, H.J.3
  • 17
    • 1942424985 scopus 로고    scopus 로고
    • Preparation of corn gluten hydrolysate with angiotensin I converting enzyme inhibitory activity and its solubility and moisture sorption
    • Kim JM, Whang JH, Kim KM, Koh JH, Suh HJ (2004) Preparation of corn gluten hydrolysate with angiotensin I converting enzyme inhibitory activity and its solubility and moisture sorption. Process Biochem 39:989-994
    • (2004) Process Biochem , vol.39 , pp. 989-994
    • Kim, J.M.1    Whang, J.H.2    Kim, K.M.3    Koh, J.H.4    Suh, H.J.5
  • 18
    • 34047257665 scopus 로고    scopus 로고
    • In vitro release of angiotensin-converting enzyme inhibitors, peroxyl-radical scavengers and antibacterial compounds by enzymatic hydrolysis of glycated gluten
    • del Castillo MD, Ferrigno A, Acampa I, Borrelli RC, Olano A, Martínez-Rodríguez A, Fogliano V (2007) In vitro release of angiotensin-converting enzyme inhibitors, peroxyl-radical scavengers and antibacterial compounds by enzymatic hydrolysis of glycated gluten. J Cereal Sci 45:327-334
    • (2007) J Cereal Sci , vol.45 , pp. 327-334
    • del Castillo, M.D.1    Ferrigno, A.2    Acampa, I.3    Borrelli, R.C.4    Olano, A.5    Martínez-Rodríguez, A.6    Fogliano, V.7
  • 19
    • 32344435383 scopus 로고    scopus 로고
    • Grain legume proteins and nutraceutical properties
    • Duranti M (2006) Grain legume proteins and nutraceutical properties. Fitoterapia 77:67-82
    • (2006) Fitoterapia , vol.77 , pp. 67-82
    • Duranti, M.1
  • 22
    • 0036219595 scopus 로고    scopus 로고
    • Characterization of inhibition and stability of soy-protein-derived angiotensin I-converting enzyme inhibitory peptides
    • Wu J, Ding X (2002) Characterization of inhibition and stability of soy-protein-derived angiotensin I-converting enzyme inhibitory peptides. Food Res Int 35:367-375
    • (2002) Food Res Int , vol.35 , pp. 367-375
    • Wu, J.1    Ding, X.2
  • 23
    • 13544276309 scopus 로고    scopus 로고
    • Direct spectrophotometric measurement of angiotensin I-converting enzyme inhibitory activity for screening bioactive peptides
    • Li G-H, Liu H, Shi YH, Le GW (2005) Direct spectrophotometric measurement of angiotensin I-converting enzyme inhibitory activity for screening bioactive peptides. J Pharm Biomed 37:219-224
    • (2005) J Pharm Biomed , vol.37 , pp. 219-224
    • Li, G.-H.1    Liu, H.2    Shi, Y.H.3    Le, G.W.4
  • 24
    • 0036302694 scopus 로고    scopus 로고
    • Utilisation of chickpea protein isolates for production of peptides with Angiotensin I-converting enzyme (ACE)-inhibitory activity
    • Pedroche J, Yust MM, Girón-Calle J, Alaiz M, Millán F, Vioque J (2002) Utilisation of chickpea protein isolates for production of peptides with Angiotensin I-converting enzyme (ACE)-inhibitory activity. J Sci Food Agric 82:960-965
    • (2002) J Sci Food Agric , vol.82 , pp. 960-965
    • Pedroche, J.1    Yust, M.M.2    Girón-Calle, J.3    Alaiz, M.4    Millán, F.5    Vioque, J.6
  • 25
    • 0042835787 scopus 로고    scopus 로고
    • Release of Angiotensin I Converting Enzyme (ACE) inhibitory activity during in vitro gastrointestinal digestion: From batch experiment to semicontinuous model
    • Vermeirssen V, Van Camp J, Devos L, Verstraete W (2003) Release of Angiotensin I Converting Enzyme (ACE) inhibitory activity during in vitro gastrointestinal digestion: from batch experiment to semicontinuous model. J Agric Food Chem 51:5680-5687
    • (2003) J Agric Food Chem , vol.51 , pp. 5680-5687
    • Vermeirssen, V.1    van Camp, J.2    Devos, L.3    Verstraete, W.4
  • 28
    • 0000193993 scopus 로고    scopus 로고
    • An in vitro method to simulate phenolic compound release from the food matrix in the gastrointestinal tract
    • Gil-Izquierdo A, Zafrilla P, Tomás-Barberán FA (2002) An in vitro method to simulate phenolic compound release from the food matrix in the gastrointestinal tract. Eur Food Res Technol 214:155-159
    • (2002) Eur Food Res Technol , vol.214 , pp. 155-159
    • Gil-Izquierdo, A.1    Zafrilla, P.2    Tomás-Barberán, F.A.3
  • 29
    • 0002739120 scopus 로고
    • In: Harris ELV, Angal S (eds), P. Imprenta, Oxford
    • Dunn MJ (1995) In: Harris ELV, Angal S (eds) Protein purification methods. P. Imprenta, Oxford
    • (1995) Protein Purification Methods
    • Dunn, M.J.1
  • 30
    • 0032854711 scopus 로고    scopus 로고
    • Effects of isolation technique and conditions on the extractability, physicochemical and functional properties of pigeonpea (Cajanus cajan) and cowpea (Vigna unguiculata) protein isolates
    • Mwasaru MA, Muhammad K, Bakar J, Che Man YB (1999) Effects of isolation technique and conditions on the extractability, physicochemical and functional properties of pigeonpea (Cajanus cajan) and cowpea (Vigna unguiculata) protein isolates. I. Physicochemical properties. Food Chem 67:435-443
    • (1999) I. Physicochemical Properties. Food Chem , vol.67 , pp. 435-443
    • Mwasaru, M.A.1    Muhammad, K.2    Bakar, J.3    Che Man, Y.B.4
  • 31
    • 34147111336 scopus 로고    scopus 로고
    • Isolation, fractionation and characterisation of proteins from Mucuna bean
    • Adebowale YA, Adeyemi IA, Oshodi AA, Niranjan K (2007) Isolation, fractionation and characterisation of proteins from Mucuna bean. Food Chem 104:287-299
    • (2007) Food Chem , vol.104 , pp. 287-299
    • Adebowale, Y.A.1    Adeyemi, I.A.2    Oshodi, A.A.3    Niranjan, K.4
  • 32
    • 43849107107 scopus 로고    scopus 로고
    • Thermal denaturation and gelation of vicilinrich protein isolates from three Phaseolus legumes: A comparative study
    • Tang C-H (2008) Thermal denaturation and gelation of vicilinrich protein isolates from three Phaseolus legumes: a comparative study. LWT-Food Sci Technol 41:1380-1388
    • (2008) LWT-Food Sci Technol , vol.41 , pp. 1380-1388
    • Tang, C.-H.1
  • 33
    • 33847030328 scopus 로고    scopus 로고
    • Antioxidant activity of protein extracts from heat-treated or thermally processed chickpeas and white beans
    • Arcan I, Yemenicioǧlu A (2007) Antioxidant activity of protein extracts from heat-treated or thermally processed chickpeas and white beans. Food Chem 103:301-312
    • (2007) Food Chem , vol.103 , pp. 301-312
    • Arcan, I.1    Yemenicioǧlu, A.2
  • 35
    • 57749110515 scopus 로고    scopus 로고
    • Effect of thermal treatment on the enzymatic hydrolysis of chicken proteins
    • Cui C, Zhou X, Zhao M, Yang B (2009) Effect of thermal treatment on the enzymatic hydrolysis of chicken proteins. Innov Food Sci Emerg 10:37-41
    • (2009) Innov Food Sci Emerg , vol.10 , pp. 37-41
    • Cui, C.1    Zhou, X.2    Zhao, M.3    Yang, B.4
  • 36
    • 57849148533 scopus 로고    scopus 로고
    • Angiotensin converting enzyme inhibitory activity of proteolytic digests of peanut (Arachis hypogaea L.) flour
    • Quist EE, Phillips RD, Saalia FK (2009) Angiotensin converting enzyme inhibitory activity of proteolytic digests of peanut (Arachis hypogaea L.) flour. LWT-Food Sci Technol 42:694-699
    • (2009) LWT-Food Sci Technol , vol.42 , pp. 694-699
    • Quist, E.E.1    Phillips, R.D.2    Saalia, F.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.