메뉴 건너뛰기




Volumn 22, Issue 6, 2013, Pages 1531-1537

Optimization of process conditions for production of angiotensin I-converting enzyme (ACE) inhibitory peptides from vital wheat gluten using response surface methodology

Author keywords

ACE inhibitory activity; degree of hydrolysis; optimization; response surface methodology; vital wheat gluten

Indexed keywords

BEVERAGES; ENZYMES; OPTIMIZATION; PEPTIDES; SURFACE PROPERTIES;

EID: 84890898244     PISSN: 12267708     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10068-013-0248-9     Document Type: Article
Times cited : (32)

References (30)
  • 1
    • 33846230958 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of wheat gluten by proteases and properties of the resulting hydrolysates
    • Kong X, Zhou H, Qian H. Enzymatic hydrolysis of wheat gluten by proteases and properties of the resulting hydrolysates. Food Chem. 102: 759-763 (2007).
    • (2007) Food Chem. , vol.102 , pp. 759-763
    • Kong, X.1    Zhou, H.2    Qian, H.3
  • 2
    • 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. Hypotensive activity of muscle protein and gluten hydrolysates obtained by protease treatment. J. Food Biochem. 26: 391-401 (2007).
    • (2007) 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
  • 3
    • 0242467926 scopus 로고    scopus 로고
    • Isolation and characterization of angiotensin Iconverting enzyme inhibitory peptides from wheat gliadin hydrolysate
    • Motoi H, Kodama T. Isolation and characterization of angiotensin Iconverting enzyme inhibitory peptides from wheat gliadin hydrolysate. Nahrung. 47: 354-358 (2003).
    • (2003) Nahrung. , vol.47 , pp. 354-358
    • Motoi, H.1    Kodama, T.2
  • 4
    • 79955469107 scopus 로고    scopus 로고
    • Antihypertensive peptides: Production, bioavailability and incorporation into foods
    • Hernández-Ledesma B, Del Mar Contreras M, Recio I. Antihypertensive peptides: Production, bioavailability and incorporation into foods. Adv. Colloid. Interfac. 165: 23-35 (2011).
    • (2011) Adv. Colloid. Interfac. , vol.165 , pp. 23-35
    • Hernández-Ledesma, B.1    Del Mar Contreras, M.2    Recio, I.3
  • 5
    • 84856818496 scopus 로고    scopus 로고
    • Microplate kinetic assay of ACE activity and response surface methodology of hydrolysis factors of peanut and cowpea flours by alcalase
    • Cuie G, Phillips R. Microplate kinetic assay of ACE activity and response surface methodology of hydrolysis factors of peanut and cowpea flours by alcalase. J. Food Agr. Environ. 10: 58-63 (2012).
    • (2012) J. Food Agr. Environ. , vol.10 , pp. 58-63
    • Cuie, G.1    Phillips, R.2
  • 7
    • 79951513633 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory properties of lentil protein hydrolysates: Determination of the kinetics of inhibition
    • Barbana C, Boye JI. Angiotensin I-converting enzyme inhibitory properties of lentil protein hydrolysates: Determination of the kinetics of inhibition. Food Chem. 127: 94-101 (2011).
    • (2011) Food Chem. , vol.127 , pp. 94-101
    • Barbana, C.1    Boye, J.I.2
  • 8
    • 31444453419 scopus 로고    scopus 로고
    • Validated ligand mapping of ACE active site
    • Kuster DJ, Marshall GR. Validated ligand mapping of ACE active site. J. Comput Aid Mol. Des. 19: 609-615 (2005).
    • (2005) J. Comput Aid Mol. Des. , vol.19 , pp. 609-615
    • Kuster, D.J.1    Marshall, G.R.2
  • 9
    • 51049097278 scopus 로고    scopus 로고
    • The possible roles of foodderived bioactive peptides in reducing the risk of cardiovascular disease
    • Erdmann K, Cheung BW, Schröder H. The possible roles of foodderived bioactive peptides in reducing the risk of cardiovascular disease. J. Nutr. Biochem. 19: 643-654 (2008).
    • (2008) J. Nutr. Biochem. , vol.19 , pp. 643-654
    • Erdmann, K.1    Cheung, B.W.2    Schröder, H.3
  • 10
    • 85092677420 scopus 로고    scopus 로고
    • Plant flavonoids as angiotensin converting enzyme inhibitors in regulation of hypertension
    • Balasuriya BN, Rupasinghe HV. Plant flavonoids as angiotensin converting enzyme inhibitors in regulation of hypertension. Funct. Food. Health Dis. 5: 172-188 (2011).
    • (2011) Funct. Food. Health Dis. , vol.5 , pp. 172-188
    • Balasuriya, B.N.1    Rupasinghe, H.V.2
  • 11
    • 33748297647 scopus 로고    scopus 로고
    • Physiological, chemical and technological aspects of milk-protein-derived peptides with antihypertensive and ACE-inhibitory activity
    • Lopez-Fandino R, Otte J, van Camp J. Physiological, chemical and technological aspects of milk-protein-derived peptides with antihypertensive and ACE-inhibitory activity. Int. Dairy J. 16: 1277-1293 (2006).
    • (2006) Int. Dairy J. , vol.16 , pp. 1277-1293
    • Lopez-Fandino, R.1    Otte, J.2    van Camp, J.3
  • 13
    • 84934443820 scopus 로고    scopus 로고
    • Antihypertensive peptides derived from bovine casein and whey proteins
    • Saito T. Antihypertensive peptides derived from bovine casein and whey proteins. Bio. Comp. Milk 295-317 (2008).
    • (2008) Bio. Comp. Milk , pp. 295-317
    • Saito, T.1
  • 14
    • 0037679233 scopus 로고    scopus 로고
    • Preparation of angiotensin I converting enzyme inhibitor from corn gluten
    • Suh H, Whang J, Kim Y, Bae S, Noh D. Preparation of angiotensin I converting enzyme inhibitor from corn gluten. Process Biochem. 38: 1239-1244 (2003).
    • (2003) Process Biochem. , vol.38 , pp. 1239-1244
    • Suh, H.1    Whang, J.2    Kim, Y.3    Bae, S.4    Noh, D.5
  • 15
    • 34047114512 scopus 로고    scopus 로고
    • Antihypertensive effect of rice protein hydrolysate with in vitro angiotensin I-converting enzyme inhibitory activity in spontaneously hypertensive rats
    • Li GH, Qu MR, Wan JZ, You JM. Antihypertensive effect of rice protein hydrolysate with in vitro angiotensin I-converting enzyme inhibitory activity in spontaneously hypertensive rats. Asia Pac. J. Clin. Nutr. 16: 275-280 (2007).
    • (2007) Asia Pac. J. Clin. Nutr. , vol.16 , pp. 275-280
    • Li, G.H.1    Qu, M.R.2    Wan, J.Z.3    You, J.M.4
  • 16
    • 34047257665 scopus 로고    scopus 로고
    • In vitro release of angiotensinconverting 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. I In vitro release of angiotensinconverting enzyme inhibitors, peroxyl-radical scavengers and antibacterial compounds by enzymatic hydrolysis of glycated gluten. J. Cereal Sci. 45: 327-334 (2007.
    • (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.I.7
  • 17
    • 21444434772 scopus 로고    scopus 로고
    • Optimization of angiotensin I-converting enzyme (ACE) inhibition by rice dregs hydrolysates using response surface methodology
    • He GQ, Xuan GD, Ruan H, Chen QH, Xu Y. Optimization of angiotensin I-converting enzyme (ACE) inhibition by rice dregs hydrolysates using response surface methodology. J. Zhejiang Univ. Sci. 6: 508 (2005).
    • (2005) J. Zhejiang Univ. Sci. , vol.6 , pp. 508
    • He, G.Q.1    Xuan, G.D.2    Ruan, H.3    Chen, Q.H.4    Xu, Y.5
  • 18
    • 47649089068 scopus 로고    scopus 로고
    • Optimization of antioxidant peptide production from grass carp sarcoplasmic protein using response surface methodology
    • Ren J, Zhao M, Shi J, Wang J, Jiang Y, Cui C, Kakuda Y, Xue SJ. Optimization of antioxidant peptide production from grass carp sarcoplasmic protein using response surface methodology. LWTFood Sci. Technol. 41: 1624-1632 (2008).
    • (2008) LWTFood Sci. Technol. , vol.41 , pp. 1624-1632
    • Ren, J.1    Zhao, M.2    Shi, J.3    Wang, J.4    Jiang, Y.5    Cui, C.6    Kakuda, Y.7    Xue, S.J.8
  • 19
    • 80052907959 scopus 로고    scopus 로고
    • Optimisation by response surface methodology, of degree of hydrolysis and antioxidant and ACE-inhibitory activities of whey protein hydrolysates obtained with cardoon extract
    • Tavares T, Contreras M, Amorim M, Martín-Álvarez P, Pintado M, Recio I, Malcata F. Optimisation by response surface methodology, of degree of hydrolysis and antioxidant and ACE-inhibitory activities of whey protein hydrolysates obtained with cardoon extract. Int. Dairy J. 21: 926-933 (2011).
    • (2011) Int. Dairy J. , vol.21 , pp. 926-933
    • Tavares, T.1    Contreras, M.2    Amorim, M.3    Martín-Álvarez, P.4    Pintado, M.5    Recio, I.6    Malcata, F.7
  • 20
    • 0036397541 scopus 로고    scopus 로고
    • Optimisation of the angiotensin converting enzyme inhibition by whey protein hydrolysates using response surface methodology
    • van der Ven C, Gruppen H, de Bont D, Voragen AG. Optimisation of the angiotensin converting enzyme inhibition by whey protein hydrolysates using response surface methodology. Int. Dairy J. 12: 813-820 (2002).
    • (2002) Int. Dairy J. , vol.12 , pp. 813-820
    • van der Ven, C.1    Gruppen, H.2    de Bont, D.3    Voragen, A.G.4
  • 21
    • 58249134379 scopus 로고    scopus 로고
    • Optimisation of hydrolysis conditions for the production of the angiotensin I-converting enzyme (ACE) inhibitory peptides from whey protein using response surface methodology
    • Guo Y, Pan D, Tanokura M. Optimisation of hydrolysis conditions for the production of the angiotensin I-converting enzyme (ACE) inhibitory peptides from whey protein using response surface methodology. Food Chem. 114: 328-333 (2009).
    • (2009) Food Chem. , vol.114 , pp. 328-333
    • Guo, Y.1    Pan, D.2    Tanokura, M.3
  • 23
    • 33646464385 scopus 로고    scopus 로고
    • Performance of two commonly used angiotensin-converting enzyme inhibition assays using FA-PGG and HHL as substrates
    • Shalaby SM, Zakora M, Otte J. Performance of two commonly used angiotensin-converting enzyme inhibition assays using FA-PGG and HHL as substrates. J. Dairy Res. 73: 178 (2006).
    • (2006) J. Dairy Res. , vol.73 , pp. 178
    • Shalaby, S.M.1    Zakora, M.2    Otte, J.3
  • 24
    • 0018536145 scopus 로고
    • Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid
    • Adler-Nissen J. Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. J. Agr. Food Chem. 27: 1256-1262 (1979).
    • (1979) J. Agr. Food Chem. , vol.27 , pp. 1256-1262
    • Adler-Nissen, J.1
  • 25
    • 80755126523 scopus 로고    scopus 로고
    • The effect of enzymes and hydrolysis conditions on degree of hydrolysis and DPPH radical scavenging activity of whey protein hydrolysates
    • Kamau SM, Lu RR. The effect of enzymes and hydrolysis conditions on degree of hydrolysis and DPPH radical scavenging activity of whey protein hydrolysates. Curr. Res. Dairy Sci. 3: 25-35 (2011).
    • (2011) Curr. Res. Dairy Sci. , vol.3 , pp. 25-35
    • Kamau, S.M.1    Lu, R.R.2
  • 26
    • 33645758029 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitor derived from soy protein hydrolysate and produced by using membrane reactor
    • Chiang WD, Tsou MJ, Tsai ZY, Tsai TC. Angiotensin I-converting enzyme inhibitor derived from soy protein hydrolysate and produced by using membrane reactor. Food Chem. 98: 725-732 (2006).
    • (2006) Food Chem. , vol.98 , pp. 725-732
    • Chiang, W.D.1    Tsou, M.J.2    Tsai, Z.Y.3    Tsai, T.C.4
  • 27
    • 0027619613 scopus 로고
    • Inhibition of angiotensin I-converting enzyme by Bacillus licheniformis alkaline protease hydrolyzates derived from sardine muscle
    • Matsui T, Matsufuji H, Seki E, Osajima K, Nakashima M, Osajima Y. Inhibition of angiotensin I-converting enzyme by Bacillus licheniformis alkaline protease hydrolyzates derived from sardine muscle. Biosci. Biotech. Bioch. 57: 922 (1993).
    • (1993) Biosci. Biotech. Bioch. , vol.57 , pp. 922
    • Matsui, T.1    Matsufuji, H.2    Seki, E.3    Osajima, K.4    Nakashima, M.5    Osajima, Y.6
  • 28
    • 0030374960 scopus 로고    scopus 로고
    • Use of response surface methodology to describe the combined effects of pH, temperature and E/S ratio on the hydrolysis of dogfish (Squalus acanthias) muscle
    • Diniz FM, Martin AM. Use of response surface methodology to describe the combined effects of pH, temperature and E/S ratio on the hydrolysis of dogfish (Squalus acanthias) muscle. Int. J. Food Sci. Tech. 31: 419-426 (2003).
    • (2003) Int. J. Food Sci. Tech. , vol.31 , pp. 419-426
    • Diniz, F.M.1    Martin, A.M.2
  • 29
    • 43849113101 scopus 로고    scopus 로고
    • Extraction optimization of watermelon seed protein using response surface methodology
    • Wani AA, Kaur D, Ahmed I, Sogi DS. Extraction optimization of watermelon seed protein using response surface methodology. LWTFood Sci. Technol. 41: 1514-1520 (2008).
    • (2008) LWTFood Sci. Technol. , vol.41 , pp. 1514-1520
    • Wani, A.A.1    Kaur, D.2    Ahmed, I.3    Sogi, D.S.4
  • 30
    • 33646180579 scopus 로고    scopus 로고
    • Effect of temperature, alkali concentration, mixing time and meal/solvent ratio on the extraction of watermelon seed proteins-a response surface approach
    • Abas Wani A, Sogi D, Grover L, Saxena D. Effect of temperature, alkali concentration, mixing time and meal/solvent ratio on the extraction of watermelon seed proteins-a response surface approach. Biosyst. Eng. 94: 67-73 (2006).
    • (2006) Biosyst. Eng. , vol.94 , pp. 67-73
    • Abas Wani, A.1    Sogi, D.2    Grover, L.3    Saxena, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.