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Volumn 141, Issue 3, 2013, Pages 2343-2354

Effect of pretreatment on enzymatic hydrolysis of bovine collagen and formation of ACE-inhibitory peptides

Author keywords

ACE inhibition; Boiling; Collagen; DH; Enzymatic hydrolysis; High pressure

Indexed keywords

BOILING LIQUIDS; COLLAGEN; ENZYMES; HYDROLYSIS; MAMMALS; PEPTIDES;

EID: 84879217402     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2013.05.058     Document Type: Article
Times cited : (118)

References (63)
  • 1
    • 33845199635 scopus 로고    scopus 로고
    • Relative amounts of tissues in mature wheat (Triticum aestivum L.) grain and their carbohydrate and phenolic acid composition
    • DOI 10.1016/j.jcs.2006.07.004, PII S0733521006000907
    • Barron, C., Surget, A., & Rouau, X. (2007). Relative amounts of tissues in mature wheat (Triticum aestivum l.) grain and their carbohydrate and phenolic acid composition. Journal of Cereal Science, 45, 88-96. (Pubitemid 44855336)
    • (2007) Journal of Cereal Science , vol.45 , Issue.1 , pp. 88-96
    • Barron, C.1    Surget, A.2    Rouau, X.3
  • 2
    • 61849147529 scopus 로고    scopus 로고
    • US Patent Application Publication US 2005/0103907 A1. Applicant, Buhler AG
    • Bohm, A., & Kratzer, A. (2005). Method for isolating aleurone particles. US Patent Application Publication US 2005/0103907 A1. Applicant, Buhler AG.
    • (2005) Method for Isolating Aleurone Particles
    • Bohm, A.1    Kratzer, A.2
  • 4
    • 7044220355 scopus 로고    scopus 로고
    • Description and characterization of wheat aleurone
    • Buri, R. C., von Reding, W., & Gavin, M. H. (2004). Description and characterization of wheat aleurone. Cereal Foods World, 49, 274-282. (Pubitemid 39416888)
    • (2004) Cereal Foods World , vol.49 , Issue.5 , pp. 274-282
    • Buri, R.C.1    Von Reding, W.2    Gavin, M.H.3
  • 5
    • 84861731831 scopus 로고    scopus 로고
    • Antioxidant phenolics of millet control lipid peroxidation in human ldl cholesterol and food system
    • Chandrasekara, A., & Shahidi, F. (2012). Antioxidant phenolics of millet control lipid peroxidation in human LDL cholesterol and food system. Journal of the American Oil Chemists' Society, 89, 275-285.
    • (2012) Journal of the American Oil Chemists' Society , vol.89 , pp. 275-285
    • Chandrasekara, A.1    Shahidi, F.2
  • 6
    • 0001988724 scopus 로고
    • Microscopic structure of the wheat grain
    • In Y. Pomeranz (Ed.). Minnesota: American Association of Cereal Chemists
    • Evers, A. D., & Bechtel, D. B. (1988). Microscopic structure of the wheat grain. In Y. Pomeranz (Ed.). Wheat: chemistry and technology (Volume I, pp. 47-95). Minnesota: American Association of Cereal Chemists.
    • (1988) Wheat: Chemistry and Technology , vol.1 , pp. 47-95
    • Evers, A.D.1    Bechtel, D.B.2
  • 7
    • 0028892406 scopus 로고
    • Release of ferulic acid from wheat bran by a ferulic acid esterase (fae-iii) from aspergillus niger
    • Faulds, C. B., & Williamson, G. (1995). Release of ferulic acid from wheat bran by a ferulic acid esterase (FAE-III) from Aspergillus niger. Applied Microbiology and Biotechnology, 43, 1082-1087.
    • (1995) Applied Microbiology and Biotechnology , vol.43 , pp. 1082-1087
    • Faulds, C.B.1    Williamson, G.2
  • 8
    • 0033028154 scopus 로고    scopus 로고
    • Antioxidant properties of 4,4'-dihydroxy-3,3'-dimethoxy-β,β'- bicinnamic acid (8-8-diferulic acid, non-cyclic form)
    • DOI 10.1002/(SICI)1097-0010(19990301)79:3<379::AID-JSFA259>3.0. CO;2-V
    • Garcia-Conesa, M. T., Wilson, P. D., Plumb, G. W., Ralph, J., & Williamson, G. (1999). Antioxidant properties of 4,4'-dihydroxy-3,3'-dimethoxy- b, b'-bicinnamic acid (8-8-diferulic acid, non-cyclic form). Journal of the Science of Food and Agriculture, 79, 379-384. (Pubitemid 29150580)
    • (1999) Journal of the Science of Food and Agriculture , vol.79 , Issue.3 , pp. 379-384
    • Garcia-Conesa, M.T.1    Wilson, P.D.2    Plumb, G.W.3    Ralph, J.4    Williamson, G.5
  • 9
    • 35548941182 scopus 로고    scopus 로고
    • Dry processes to develop wheat fractions and products with enhanced nutritional quality
    • DOI 10.1016/j.jcs.2007.09.008, PII S0733521007001737
    • Hemery, Y., Rouau, X., Lullien-Pellerin, V., Barron, C., & Abecassis, J. (2007). Dry processes to develop wheat fractions and products with enhanced nutritional quality. Journal of Cereal Science, 46, 327-347. (Pubitemid 350011034)
    • (2007) Journal of Cereal Science , vol.46 , Issue.3 , pp. 327-347
    • Hemery, Y.1    Rouau, X.2    Lullien-Pellerin, V.3    Barron, C.4    Abecassis, J.5
  • 10
    • 77953915850 scopus 로고    scopus 로고
    • Dry-fractionation of wheat bran increases the bioaccessibility of phenolic acids in breads made from processed bran fractions
    • Hemery, Y., Mateo Anson, N., Havenaar, R., Haenen, G.R.M.M., Noort, M.W.J., & Rouau, X. (2010). Dry-fractionation of wheat bran increases the bioaccessibility of phenolic acids in breads made from processed bran fractions. Food Research International, 43, 1429-1438
    • (2010) Food Research International , vol.43 , pp. 1429-1438
    • Hemery, Y.1    Mateo Anson, N.2    Havenaar, R.3    Haenen, G.R.M.M.4    Noort, M.W.J.5    Rouau, X.6
  • 11
    • 84884586510 scopus 로고    scopus 로고
    • ICC-Standards.; No. 128: Procedure for the determination of starch after enzymatic decomposition (1998); No. 167: Determination of crude protein in grain and grain products for food and feed by the Dumas combustion principle (2000
    • ICC-Standards. (1994). No. 104: Determination of ash in cereals and cereal products (1990); No. 128: Procedure for the determination of starch after enzymatic decomposition (1998); No. 167: Determination of crude protein in grain and grain products for food and feed by the Dumas combustion principle (2000).
    • No. 104: Determination of Ash in Cereals and Cereal Products (1990 , vol.1994
  • 12
    • 3142570262 scopus 로고
    • A simple and colorimetric method for phytate determination
    • Latta, M., & Eskin, M. (1980). A simple and colorimetric method for phytate determination. Journal of Agricultural and Food Chemistry, 28, 1315-1317.
    • (1980) Journal of Agricultural and Food Chemistry , vol.28 , pp. 1315-1317
    • Latta, M.1    Eskin, M.2
  • 13
    • 58149345880 scopus 로고    scopus 로고
    • Phenolic acids in wheat varieties in the healthgrain diversity screen
    • Li, L., Shewry, P. R., & Ward, J. L. (2008). Phenolic acids in wheat varieties in the HEALTHGRAIN diversity screen. Journal of Agricultural and Food Chemistry, 56, 9732-9739.
    • (2008) Journal of Agricultural and Food Chemistry , vol.56 , pp. 9732-9739
    • Li, L.1    Shewry, P.R.2    Ward, J.L.3
  • 14
    • 75249097116 scopus 로고    scopus 로고
    • Chemical modeling of hemeinduced lipid oxidation in gastric conditions and inhibition by dietary polyphenols
    • Lorrain, B., Dangles, O., Genot, C., & Dufour, C. (2010). Chemical modeling of hemeinduced lipid oxidation in gastric conditions and inhibition by dietary polyphenols. Journal of Agricultural and Food Chemistry, 58, 676-683.
    • (2010) Journal of Agricultural and Food Chemistry , vol.58 , pp. 676-683
    • Lorrain, B.1    Dangles, O.2    Genot, C.3    Dufour, C.4
  • 15
    • 34447303337 scopus 로고    scopus 로고
    • Antioxidative and antiproliferative properties of selected barley (Hordeum vulgarae L.) cultivars and their potential for inhibition of Low-Density Lipoprotein (LDL) cholesterol oxidation
    • DOI 10.1021/jf070072a
    • Madhujith, T., & Shahidi, F. (2007). Antioxidative and antiproliferative properties of selected barley (Hordeum vulgare L.) Cultivars and their potential for inhibition of low-density lipoprotein (LDL) cholesterol oxidation. Journal of Agricultural and Food Chemistry, 55, 5018-5024. (Pubitemid 47056051)
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , Issue.13 , pp. 5018-5024
    • Madhujith, T.1    Shahidi, F.2
  • 19
    • 0034865748 scopus 로고    scopus 로고
    • Release of ferulic acid from cereal residues by barley enzymatic extracts
    • DOI 10.1006/jcrs.2001.0386
    • Sancho, A. I., Bartolomé, B., Gomez-Cordovés, C., Williamson, G., & Faulds, C. B. (2001). Release of ferulic acid from cereal residues by barley enzymatic extracts. Journal of Cereal Science, 34, 173-179. (Pubitemid 32792820)
    • (2001) Journal of Cereal Science , vol.34 , Issue.2 , pp. 173-179
    • Sancho, A.I.1    Bartolome, B.2    Gomez-Cordoves, C.3    Williamson, G.4    Faulds, C.B.5
  • 20
    • 1542749829 scopus 로고    scopus 로고
    • A procedure to measure the antiradical efficiency of polyphenols
    • DOI 10.1002/(SICI)1097-0010(199802)76:2<270::AID-JSFA945>3.0.CO;2-9
    • Sanchèz-Moreno, C., Larrauri, J. A., & Saura-Calixto, F. (1998). A procedure to measure the antiradical efficiency of polyphenols. Journal of the Science of Food and Agriculture, 76, 270-276. (Pubitemid 28126648)
    • (1998) Journal of the Science of Food and Agriculture , vol.76 , Issue.2 , pp. 270-276
    • Sanchez-Moreno, C.1    Larrauri, J.A.2    Saura-Calixto, F.3
  • 21
    • 70349987101 scopus 로고    scopus 로고
    • Phytate in foods and significance for humans: Food sources, intake, processing, bioavailability, protective role and analysis
    • Schlemmer, U., Frølich, W., Prieto, R. M., & Grases, F. (2009). Phytate in foods and significance for humans: Food sources, intake, processing, bioavailability, protective role and analysis. Molecular Nutrition & Food Research, 53, S330-S375.
    • (2009) Molecular Nutrition & Food Research , vol.53
    • Schlemmer, U.1    Frølich, W.2    Prieto, R.M.3    Grases, F.4
  • 22
    • 54849426374 scopus 로고    scopus 로고
    • Direct measurement of the total antioxidant capacity of cereal products
    • Serpen, A., Gökmen, V., Pellegrini, N., & Fogliano, V. (2008). Direct measurement of the total antioxidant capacity of cereal products. Journal of Cereal Science, 48, 816-820.
    • (2008) Journal of Cereal Science , vol.48 , pp. 816-820
    • Serpen, A.1    Gökmen, V.2    Pellegrini, N.3    Fogliano, V.4
  • 23
    • 0024289327 scopus 로고
    • Colorimetric determination of phytate in unpurified extracts of seeds and the products of their processing
    • Vaintraub, I. A., & Lapteva, N. A. (1988). Colorimetric determination of phytate in unpurified extracts of seeds and the products of their processing. Analytical Biochemistry, 175, 227-230.
    • (1988) Analytical Biochemistry , vol.175 , pp. 227-230
    • Vaintraub, I.A.1    Lapteva, N.A.2
  • 24
    • 0037070363 scopus 로고    scopus 로고
    • Release of ferulic acid from oat hulls by Aspergillus ferulic acid esterase and Trichoderma xylanase
    • DOI 10.1021/jf010984r
    • Yu, P., Maenz, D. D., McKinnon, J. J., Racz, V. J., & Christensen, D. A. (2002). Release of ferulic acid from oat hulls by Aspergillus ferulic acid esterase and Trichoderma xylanase. Journal of Agricultural and Food Chemistry, 50, 1625-1630. (Pubitemid 34233236)
    • (2002) Journal of Agricultural and Food Chemistry , vol.50 , Issue.6 , pp. 1625-1630
    • Yu, P.1    Maenz, D.D.2    McKinnon, J.J.3    Racz, V.J.4    Christensen, D.A.5
  • 25
    • 41549123951 scopus 로고    scopus 로고
    • Chemistry, natural sources, dietary intake and pharmacokinetic properties of ferulic acid: A review
    • Zhao, Z., & Moghadasian, M. H. (2008). Chemistry, natural sources, dietary intake and pharmacokinetic properties of ferulic acid: A review. Food Chemistry, 109(4), 691-702.
    • (2008) Food Chemistry , vol.109 , Issue.4 , pp. 691-702
    • Zhao, Z.1    Moghadasian, M.H.2
  • 26
    • 1542317484 scopus 로고    scopus 로고
    • Comparison of swiss red wheat grain and fractions for their antioxidant properties
    • Zhou, K., Laux, J., & Yu, L. (2004). Comparison of swiss red wheat grain and fractions for their antioxidant properties. Journal of Agricultural and Food Chemistry, 52, 1118-1123.
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , pp. 1118-1123
    • Zhou, K.1    Laux, J.2    Yu, L.3
  • 27
    • 0016701302 scopus 로고
    • The covalent structure of collagen. The aminoacid sequence of alpha2-cb4 from calf-skin collagen
    • Fietzek, P. P., & Rexrodt, F. W. (1975). The covalent structure of collagen. The aminoacid sequence of alpha2-CB4 from calf-skin collagen. European Journal of Biochemistry, 59(1), 113-118.
    • (1975) European Journal of Biochemistry , vol.59 , Issue.1 , pp. 113-118
    • Fietzek, P.P.1    Rexrodt, F.W.2
  • 28
    • 79961026637 scopus 로고    scopus 로고
    • Functional and bioactive properties of collagen and gelatin from alternative sources: A review
    • Gomez-Guillen, M. C., Gimenez, B., Lopez-Caballero, M. E., & Montero, M. P. (2011). Functional and bioactive properties of collagen and gelatin from alternative sources: A review. Food Hydrocolloids, 25(8), 1813-1827.
    • (2011) Food Hydrocolloids , vol.25 , Issue.8 , pp. 1813-1827
    • Gomez-Guillen, M.C.1    Gimenez, B.2    Lopez-Caballero, M.E.3    Montero, M.P.4
  • 29
    • 17544377011 scopus 로고    scopus 로고
    • Extraction of gelatin from fish skins by high pressure treatment
    • DOI 10.1016/j.foodhyd.2004.12.011
    • Gomez-Guillen, M. C., Gimenez, B., & Montero, P. (2005). Extraction of gelatin from fish skins by high pressure treatment. Food Hydrocolloids, 19(5), 923-928. (Pubitemid 40552868)
    • (2005) Food Hydrocolloids , vol.19 , Issue.5 , pp. 923-928
    • Gomez-Guillen, M.C.1    Gimenez, B.2    Montero, P.3
  • 30
    • 0036132846 scopus 로고    scopus 로고
    • Structural and physical properties of gelatin extracted from different marine species: A comparative study
    • DOI 10.1016/S0268-005X(01)00035-2, PII S0268005X01000352
    • Gomez-Guillen, M. C., Turnay, J., Fernandez-Diaz, M. D., Ulmo, N., Lizarbe, M. A., & Montero, P. (2002). Structural and physical properties of gelatin extracted from different marine species: A comparative study. Food Hydrocolloids, 16(1), 25-34. (Pubitemid 33134723)
    • (2002) Food Hydrocolloids , vol.16 , Issue.1 , pp. 25-34
    • Gomez-Guillen, M.C.1    Turnay, J.2    Fernandez-Diaz, M.D.3    Ulmo, N.4    Lizarbe, M.A.5    Montero, P.6
  • 31
    • 84861096488 scopus 로고    scopus 로고
    • High pressure treatment of brine enhanced pork affects endopeptidase activity, protein solubility, and peptide formation
    • Grossi, A., Gkarane, V., Otte, J. A., Ertbjerg, P., & Orlien, V. (2012). High pressure treatment of brine enhanced pork affects endopeptidase activity, protein solubility, and peptide formation. Food Chemistry, 134(3), 1556-1563.
    • (2012) Food Chemistry , vol.134 , Issue.3 , pp. 1556-1563
    • Grossi, A.1    Gkarane, V.2    Otte, J.A.3    Ertbjerg, P.4    Orlien, V.5
  • 34
    • 75449100518 scopus 로고    scopus 로고
    • Hydroxyproline-containing dipeptides and tripeptides quantified at high concentration in human blood after oral administration of gelatin hydrolysate
    • Ichikawa, S., Morifuji, M., Ohara, H., Matsumoto, H., Takeuchi, Y., & Sato, K. (2010). Hydroxyproline-containing dipeptides and tripeptides quantified at high concentration in human blood after oral administration of gelatin hydrolysate. International Journal of Food Sciences and Nutrition, 61(1), 52-60.
    • (2010) International Journal of Food Sciences and Nutrition , vol.61 , Issue.1 , pp. 52-60
    • Ichikawa, S.1    Morifuji, M.2    Ohara, H.3    Matsumoto, H.4    Takeuchi, Y.5    Sato, K.6
  • 35
    • 70350446613 scopus 로고    scopus 로고
    • Antihypertensive effect of enzymatic hydrolysate of collagen and gly-pro in spontaneously hypertensive rats
    • Ichimura, T., Yamanaka, A., Otsuka, T., Yamashita, E., & Maruyama, S. (2009). Antihypertensive effect of enzymatic hydrolysate of collagen and Gly-Pro in spontaneously hypertensive rats. Bioscience Biotechnology and Biochemistry, 73(10), 2317-2319.
    • (2009) Bioscience Biotechnology and Biochemistry , vol.73 , Issue.10 , pp. 2317-2319
    • Ichimura, T.1    Yamanaka, A.2    Otsuka, T.3    Yamashita, E.4    Maruyama, S.5
  • 36
    • 33748349239 scopus 로고    scopus 로고
    • Tenderizing effect of high hydrostatic pressure bovine intramuscular connective tissue
    • Ichinoseki, S., Nishiumi, T., & Suzuki, A. (2006). Tenderizing effect of high hydrostatic pressure bovine intramuscular connective tissue. Journal of Food Science, 71(6), 276-281.
    • (2006) Journal of Food Science , vol.71 , Issue.6 , pp. 276-281
    • Ichinoseki, S.1    Nishiumi, T.2    Suzuki, A.3
  • 38
    • 0034840775 scopus 로고    scopus 로고
    • Angiotensin I converting enzyme inhibitory peptides purified from bovine skin gelatin hydrolysate
    • Kim, S. K., Byun, H. G., Park, P. J., & Shahidi, F. (2001). Angiotensin I converting enzyme inhibitory peptides purified from bovine skin gelatin hydrolysate. Journal of Agricultural and Food Chemistry, 49(6), 2992-2997. (Pubitemid 32826100)
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , Issue.6 , pp. 2992-2997
    • Kim, S.-K.1    Byun, H.-G.2    Park, P.-J.3    Shahidi, F.4
  • 39
    • 0036397747 scopus 로고    scopus 로고
    • Effect of high hydrostatic pressure on the conformation of β-lactoglobulin A as assessed by proteolytic peptide profiling
    • DOI 10.1016/S0958-6946(02)00078-X, PII S095869460200078X
    • Knudsen, J. C., Otte, J., Olsen, K., & Skibsted, L. H. (2002). Effect of high hydrostatic pressure on the conformation of beta-lactoglobulin A as assessed by proteolytic peptide profiling. International Dairy Journal, 12(10), 791-803. (Pubitemid 35180615)
    • (2002) International Dairy Journal , vol.12 , Issue.10 , pp. 791-803
    • Knudsen, J.C.1    Otte, J.2    Olsen, K.3    Skibsted, L.H.4
  • 40
    • 36148941334 scopus 로고    scopus 로고
    • Effect of extracting time and temperature on yield of gelatin from different fish offal
    • DOI 10.1016/j.foodchem.2007.08.071, PII S0308814607008928
    • Kolodziejska, I., Skierka, E., Sadowska, M., Kolodziejski, W., & Niecikowska, C. (2008). Effect of extracting time and temperature on yield of gelatin from different fish offal. Food Chemistry, 107(2), 700-706. (Pubitemid 350116374)
    • (2008) Food Chemistry , vol.107 , Issue.2 , pp. 700-706
    • Kolodziejska, I.1    Skierka, E.2    Sadowska, M.3    Kolodziejski, W.4    Niecikowska, C.5
  • 41
    • 79957447420 scopus 로고    scopus 로고
    • Optimization of hydrolysis conditions for the production of the angiotensin-i converting enzyme inhibitory peptides from sea cucumber collagen hydrolysates
    • Liu, Z. Y., Chen, D., Su, Y. C., & Zeng, M. Y. (2011). Optimization of hydrolysis conditions for the production of the angiotensin-I converting enzyme inhibitory peptides from sea cucumber collagen hydrolysates. Journal of Aquatic Food Product Technology, 20(2), 222-232.
    • (2011) Journal of Aquatic Food Product Technology , vol.20 , Issue.2 , pp. 222-232
    • Liu, Z.Y.1    Chen, D.2    Su, Y.C.3    Zeng, M.Y.4
  • 42
    • 79952353155 scopus 로고    scopus 로고
    • Bovine meat proteins as potential precursors of biologically active peptides-A computational study based on the biopep database
    • Minkiewicz, P., Dziuba, J., & Michalska, J. (2011). Bovine meat proteins as potential precursors of biologically active peptides-A computational study based on the BIOPEP database. Food Science and Technology International, 17(1), 39-45.
    • (2011) Food Science and Technology International , vol.17 , Issue.1 , pp. 39-45
    • Minkiewicz, P.1    Dziuba, J.2    Michalska, J.3
  • 44
    • 0036660813 scopus 로고    scopus 로고
    • Development of an effective process for utilization of collagen from livestock and fish waste
    • DOI 10.1016/S0032-9592(02)00024-9, PII S0032959202000249
    • Morimura, S., Nagata, H., Uemura, Y., Fahmi, A., Shigematsu, T., & Kida, K. (2002). Development of an effective process from livestock and for utilization of collagen fish waste. Process Biochemistry, 37(12), 1403-1412. (Pubitemid 35192004)
    • (2002) Process Biochemistry , vol.37 , Issue.12 , pp. 1403-1412
    • Morimura, S.1    Nagata, H.2    Uemura, Y.3    Fahmi, A.4    Shigematsu, T.5    Kida, K.6
  • 45
    • 43049088866 scopus 로고    scopus 로고
    • Molecular and physical characteristics of squid (Todarodes pacificus) skin collagens and biological properties of their enzymatic hydrolysates
    • DOI 10.1111/j.1750-3841.2008.00722.x
    • Nam, K. A., You, S. G., & Kim, S. M. (2008). Molecular and physical characteristics of squid (Todarodes pacificus) skin collagens and biological properties of their enzymatic hydrolysates. Journal of Food Science, 73(4), C249-C255. (Pubitemid 351629811)
    • (2008) Journal of Food Science , vol.73 , Issue.4
    • Nam, K.A.1    You, S.G.2    Kim, S.M.3
  • 46
    • 57449087412 scopus 로고    scopus 로고
    • Peptide profiles and angiotensin-i-converting enzyme inhibitory activity of fermented milk products: Effect of bacterial strain, fermentation ph, and storage time
    • Nielsen, M. S., Martinussen, T., Flambard, B., Sørensen, K. I., & Otte, J. (2009). Peptide profiles and angiotensin-I-converting enzyme inhibitory activity of fermented milk products: Effect of bacterial strain, fermentation pH, and storage time. International Dairy Journal, 19, 155-165.
    • (2009) International Dairy Journal , vol.19 , pp. 155-165
    • Nielsen, M.S.1    Martinussen, T.2    Flambard, B.3    Sørensen, K.I.4    Otte, J.5
  • 47
    • 0018305067 scopus 로고
    • Peptide inhibitors of angiotensin I-converting enzyme in digests of gelatin by bacterial collagenase
    • Oshima, G., Shimabukuro, H., & Nagasawa, K. (1979). Peptide inhibitors of angiotensin I-converting enzyme in digests of gelatin by bacterial collagenase. Biochimica et Biophysica Acta, 566(1), 128-137. (Pubitemid 9076461)
    • (1979) Biochimica et Biophysica Acta , vol.566 , Issue.1 , pp. 128-137
    • Oshima, G.1    Shimabukuro, H.2    Nagasawa, K.3
  • 48
    • 0033494695 scopus 로고    scopus 로고
    • Protease-induced gelation of unheated and heated whey proteins: Effects of pH, temperature, and concentrations of protein, enzyme and salts
    • DOI 10.1016/S0958-6946(99)00151-X, PII S095869469900151X
    • Otte, J., Schumacher, E., Ipsen, R., Ju, Z. Y., & Qvist, K. B. (1999). Protease-induced gelation of unheated and heated whey proteins: Effects of pH, temperature, and concentrations of protein, enzyme and salts. International Dairy Journal, 9(11), 801-812. (Pubitemid 30147212)
    • (1999) International Dairy Journal , vol.9 , Issue.11 , pp. 801-812
    • Otte, J.1    Schumacher, E.2    Ipsen, R.3    Ju, Z.Y.4    Qvist, K.B.5
  • 49
    • 33846024711 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme inhibitory activity of milk protein hydrolysates: Effect of substrate, enzyme and time of hydrolysis
    • DOI 10.1016/j.idairyj.2006.05.011, PII S0958694606001385
    • Otte, J., Shalaby, S. M., Zakora, M., Pripp, A. H., & EI-Shabrawy, S. A. (2007). Angiotensin-converting enzyme inhibitory activity of milk protein hydrolysates: Effect of substrate, enzyme and time of hydrolysis. International Dairy Journal, 17(5), 488-503. (Pubitemid 46043426)
    • (2007) International Dairy Journal , vol.17 , Issue.5 , pp. 488-503
    • Otte, J.1    Shalaby, S.M.2    Zakora, M.3    Pripp, A.H.4    El-Shabrawy, S.A.5
  • 51
    • 0014381820 scopus 로고
    • Interchain hydrogen bonds via bound water molecules in collagen triple helix
    • Ramachan, G. N., & Chandras, R. (1968). Interchain hydrogen bonds via bound water molecules in collagen triple helix. Biopolymers, 6(11), 1649-1658.
    • (1968) Biopolymers , vol.6 , Issue.11 , pp. 1649-1658
    • Ramachan, G.N.1    Chandras, R.2
  • 52
    • 0028175379 scopus 로고
    • Tgf-beta-1 induces the expression of type-i collagen and sparc, and enhances contraction of collagen gels, by fibroblasts from young and aged donors
    • Reed, M. J., Vernon, R. B., Abrass, I. B., & Sage, E. H. (1994). Tgf-Beta-1 induces the expression of type-I collagen and sparc, and enhances contraction of collagen gels, by fibroblasts from young and aged donors. Journal of Cellular Physiology, 158(1), 169-179.
    • (1994) Journal of Cellular Physiology , vol.158 , Issue.1 , pp. 169-179
    • Reed, M.J.1    Vernon, R.B.2    Abrass, I.B.3    Sage, E.H.4
  • 53
    • 0027417926 scopus 로고
    • Radioimmunoassay for the pyridinoline cross-linked carboxy-terminal telopeptide of type I collagen: A new serum marker of bone collagen degradation
    • Risteli, J., Elomaa, I., Niemi, S., Novamo, A., & Risteli, L. (1993). Radioimmunoassay for the pyridinoline cross-linked carboxy-Terminal telopeptide of type-i collagen-A new serum marker of bone-collagen degradation. Clinical Chemistry, 39(4), 635-640. (Pubitemid 23118314)
    • (1993) Clinical Chemistry , vol.39 , Issue.4 , pp. 635-640
    • Risteli, J.1    Elomaa, I.2    Niemi, S.3    Novamo, A.4    Risteli, L.5
  • 56
    • 34548819013 scopus 로고    scopus 로고
    • A fluorescence-based protocol for quantifying angiotensin-converting enzyme activity
    • Sentandreu, M. A., & Toldra, F. (2006). A fluorescence-based protocol for quantifying angiotensin-converting enzyme activity. Nature Protocols, 1(5), 2423-2427.
    • (2006) Nature Protocols , vol.1 , Issue.5 , pp. 2423-2427
    • Sentandreu, M.A.1    Toldra, F.2
  • 57
  • 58
    • 0038029531 scopus 로고    scopus 로고
    • Proteinase and exopeptidase hydrolysis of whey protein: Comparison of the TNBS, OPA and pH stat methods for quantification of degree of hydrolysis
    • DOI 10.1016/S0958-6946(03)00053-0
    • Spellman, D., McEvoy, E., O'Cuinn, G., & FitzGerald, R. J. (2003). Proteinase and exopeptidase hydrolysis of whey protein: Comparison of the TNBS, OPA and pH stat methods for quantification of degree of hydrolysis. International Dairy Journal, 13(6), 447-453. (Pubitemid 36579916)
    • (2003) International Dairy Journal , vol.13 , Issue.6 , pp. 447-453
    • Spellman, D.1    McEvoy, E.2    O'Cuinn, G.3    FitzGerald, R.J.4
  • 59
    • 34147121501 scopus 로고    scopus 로고
    • Effects of high pressure on functional properties of soy protein
    • DOI 10.1016/j.foodchem.2006.11.013, PII S0308814606008776
    • Torrezan, R., Tham, W. P., Bell, A. E., Frazier, R. A., & Cristianini, M. (2007). Effects of high pressure on functional properties of soy protein. Food Chemistry, 104(1), 140-147. (Pubitemid 46561109)
    • (2007) Food Chemistry , vol.104 , Issue.1 , pp. 140-147
    • Torrezan, R.1    Tham, W.P.2    Bell, A.E.3    Frazier, R.A.4    Cristianini, M.5
  • 61
    • 53949124119 scopus 로고    scopus 로고
    • Immunomodulatory effects of marine oligopeptide preparation from chum salmon (oncorhynchus keta) in mice
    • Yang, R. Y., Zhang, Z. F., Pei, X. R., Han, X. L., Wang, J. B., Wang, L. L., et al. (2009). Immunomodulatory effects of marine oligopeptide preparation from Chum Salmon (Oncorhynchus keta) in mice. Food Chemistry, 113(2), 464-470.
    • (2009) Food Chemistry , vol.113 , Issue.2 , pp. 464-470
    • Yang, R.Y.1    Zhang, Z.F.2    Pei, X.R.3    Han, X.L.4    Wang, J.B.5    Wang, L.L.6
  • 62
    • 33644597445 scopus 로고    scopus 로고
    • Physicochemical properties of collagen, gelatin and collagen hydrolysate derived from bovine limed split wastes
    • Zhang, Z. K., Li, G. Y., & Shi, B. (2006). Physicochemical properties of collagen, gelatin and collagen hydrolysate derived from bovine limed split wastes. Journal of the Society of Leather Technologists and Chemists, 90(1), 23-28.
    • (2006) Journal of the Society of Leather Technologists and Chemists , vol.90 , Issue.1 , pp. 23-28
    • Zhang, Z.K.1    Li, G.Y.2    Shi, B.3
  • 63
    • 36048952787 scopus 로고    scopus 로고
    • Antihypertensive effect and purification of an ACE inhibitory peptide from sea cucumber gelatin hydrolysate
    • DOI 10.1016/j.procbio.2007.08.011, PII S1359511307002346
    • Zhao, Y. H., Li, B. F., Liu, Z. Y., Dong, S. Y., Zhao, X., & Zeng, M. Y. (2007). Antihypertensive effect and purification of an ACE inhibitory peptide from sea cucumber gelatin hydrolysate. Process Biochemistry, 42(12), 1586-1591. (Pubitemid 350101340)
    • (2007) Process Biochemistry , vol.42 , Issue.12 , pp. 1586-1591
    • Zhao, Y.1    Li, B.2    Liu, Z.3    Dong, S.4    Zhao, X.5    Zeng, M.6


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