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Volumn 56, Issue 6, 2008, Pages 2183-2191

Susceptibility of phaseolin to in vitro proteolysis is highly variable across common bean varieties (Phaseolus vulgaris)

Author keywords

Nutritional value; Phaseolin; Phaseolus vulgaris; Proteolysis

Indexed keywords

AMINO ACID; PANCREATIN; PEPSIN A; PEPTIDE HYDROLASE; PHASEOLIN PROTEIN, PHASEOLUS VULGARIS; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

EID: 41849092668     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf072576e     Document Type: Article
Times cited : (47)

References (31)
  • 1
    • 0036983946 scopus 로고    scopus 로고
    • Factors influencing pulse consumption in Latin America
    • Leterme, P.; Muñoz, L. C. Factors influencing pulse consumption in Latin America. Br. J. Nutr. 2002, 88, S251-S254.
    • (2002) Br. J. Nutr , vol.88
    • Leterme, P.1    Muñoz, L.C.2
  • 2
    • 0036984343 scopus 로고    scopus 로고
    • Recommendations by health organizations for pulse consumption
    • Leterme, P. Recommendations by health organizations for pulse consumption. Br. J. Nutr. 2002, 88, S239-S242.
    • (2002) Br. J. Nutr , vol.88
    • Leterme, P.1
  • 4
    • 0000917494 scopus 로고
    • Seed proteins of common bean
    • Ma, Y.; Bliss, F. Seed proteins of common bean. Crop Sci. 1978, 18, 431-437.
    • (1978) Crop Sci , vol.18 , pp. 431-437
    • Ma, Y.1    Bliss, F.2
  • 5
    • 0019618248 scopus 로고
    • Composition and digestibility of albumin, globulins, and glutelins from Phaseolus vulgaris
    • Marquez, U. M.; Lajolo, F. M. Composition and digestibility of albumin, globulins, and glutelins from Phaseolus vulgaris. J. Agric. Food Chem. 1981, 29, 1068-1074.
    • (1981) J. Agric. Food Chem , vol.29 , pp. 1068-1074
    • Marquez, U.M.1    Lajolo, F.M.2
  • 7
    • 84987277329 scopus 로고
    • In vitro enzymatic hydrolysis of phaseolin, the major storage protein of Phaseolus vulgaris L
    • Deshpande, S. S.; Nielsen, S. S. In vitro enzymatic hydrolysis of phaseolin, the major storage protein of Phaseolus vulgaris L. J. Food Sci. 1987, 52, 1326-1329.
    • (1987) J. Food Sci , vol.52 , pp. 1326-1329
    • Deshpande, S.S.1    Nielsen, S.S.2
  • 8
    • 32844458708 scopus 로고    scopus 로고
    • Influence of the Phaseolus vulgaris phaseolin level of incorporation, type and thermal treatment on gut characteristics in rats
    • Montoya, C. A.; Lallès, J. P.; Beebe, S.; Montagne, L.; Souffrant, W. B.; Leterme, P. Influence of the Phaseolus vulgaris phaseolin level of incorporation, type and thermal treatment on gut characteristics in rats. Br. J. Nutr. 2006, 95, 116-123.
    • (2006) Br. J. Nutr , vol.95 , pp. 116-123
    • Montoya, C.A.1    Lallès, J.P.2    Beebe, S.3    Montagne, L.4    Souffrant, W.B.5    Leterme, P.6
  • 9
    • 0348238801 scopus 로고    scopus 로고
    • Phaseolin seed variability in common bean (Phaseolus vulgaris) by capillary gel electrophoresis
    • Salmanowicz, B. P. Phaseolin seed variability in common bean (Phaseolus vulgaris) by capillary gel electrophoresis. J. Appl. Genet. 2001, 42, 269-281.
    • (2001) J. Appl. Genet , vol.42 , pp. 269-281
    • Salmanowicz, B.P.1
  • 10
    • 0002286580 scopus 로고
    • Phaseolin as an evolutionary marker
    • Gepts, P, Ed, Kluwer Academic Publishers: Dordrecht, Holland
    • Gepts, P. Phaseolin as an evolutionary marker. In Genetic Resources of Phaseolus beans; Gepts, P., Ed.; Kluwer Academic Publishers: Dordrecht, Holland, 1988; pp 215-241..
    • (1988) Genetic Resources of Phaseolus beans , pp. 215-241
    • Gepts, P.1
  • 11
    • 0022432415 scopus 로고
    • Nucleotide sequence from phaseolin cDNA clones: The major storage proteins from Phaseolus vulgaris are encoded by two unique gene families
    • Slightom, J. L.; Drong, R. F.; Klassy, R. C.; Hoffman, L. M. Nucleotide sequence from phaseolin cDNA clones: the major storage proteins from Phaseolus vulgaris are encoded by two unique gene families. Nucleic Acids Res. 1985, 13, 6483-6498.
    • (1985) Nucleic Acids Res , vol.13 , pp. 6483-6498
    • Slightom, J.L.1    Drong, R.F.2    Klassy, R.C.3    Hoffman, L.M.4
  • 12
    • 41849092889 scopus 로고    scopus 로고
    • Montoya, C. A.; Lallès, J. P.; Beebe, S.; Souffrant, W. B.; Leterme, P. Effect of the types of Phaseolus vulgaris phaseolin and thermal treatment on in vitro sequential hydrolysis by pepsin and pancreatin. Proceedings of the Fourth International Food Legumes Research Conference, 2005, Indian Society of Genetics and Plant Breeding, New Delhi, India; Kharkwal, M. C., Ed.; Kamala Print-n-publish: New Delhi pp 61-62..
    • Montoya, C. A.; Lallès, J. P.; Beebe, S.; Souffrant, W. B.; Leterme, P. Effect of the types of Phaseolus vulgaris phaseolin and thermal treatment on in vitro sequential hydrolysis by pepsin and pancreatin. Proceedings of the Fourth International Food Legumes Research Conference, 2005, Indian Society of Genetics and Plant Breeding, New Delhi, India; Kharkwal, M. C., Ed.; Kamala Print-n-publish: New Delhi pp 61-62..
  • 13
    • 0001057226 scopus 로고
    • Resistance of the kidney bean reserve protein, phaseolin, to proteolysis in the porcine digestive tract
    • Begbie, R.; Ross, A. W. Resistance of the kidney bean reserve protein, phaseolin, to proteolysis in the porcine digestive tract. J. Sci. Food Agric. 1993, 61, 301-307.
    • (1993) J. Sci. Food Agric , vol.61 , pp. 301-307
    • Begbie, R.1    Ross, A.W.2
  • 14
    • 0000129621 scopus 로고
    • Equal expression of the maternal and paternal alleles for polypeptide subunits of the major storage protein of the bean Phaseolus vulgaris L
    • Hall, T. C.; McLeester, R. C.; Bliss, F. A. Equal expression of the maternal and paternal alleles for polypeptide subunits of the major storage protein of the bean Phaseolus vulgaris L. Plant Physiol. 1977, 59, 1122-1124.
    • (1977) Plant Physiol , vol.59 , pp. 1122-1124
    • Hall, T.C.1    McLeester, R.C.2    Bliss, F.A.3
  • 15
    • 0002788050 scopus 로고
    • In vitro and in vivo studies of the digestibility of the major storage protein of the navy bean Phaseolus vulgaris
    • Liener, I.; Thompson, R. In vitro and in vivo studies of the digestibility of the major storage protein of the navy bean Phaseolus vulgaris. Qual. Plant. Plant Foods Hum. Nutr. 1980, 30, 13-25.
    • (1980) Qual. Plant. Plant Foods Hum. Nutr , vol.30 , pp. 13-25
    • Liener, I.1    Thompson, R.2
  • 16
    • 38949150036 scopus 로고    scopus 로고
    • Phaseolin type and heat treatment influence the biochemistry of protein digestion in rat intestine
    • Montoya, C. A.; Leterme, P.; Beebe, S.; Souffrant, W. B.; Mollé, D.; Lallès, J. P. Phaseolin type and heat treatment influence the biochemistry of protein digestion in rat intestine. Br. J. Nutr. 2008, 99, 531-539.
    • (2008) Br. J. Nutr , vol.99 , pp. 531-539
    • Montoya, C.A.1    Leterme, P.2    Beebe, S.3    Souffrant, W.B.4    Mollé, D.5    Lallès, J.P.6
  • 17
    • 34548569201 scopus 로고    scopus 로고
    • In vitro and in vivo protein hydrolysis of beans (Phaseolus vulgaris) genetically modified to express different phaseolin types
    • Montoya, C. A.; Gomez, A. S.; Lallès, J. P.; Souffrant, W. B.; Beebe, S.; Leterme, P. In vitro and in vivo protein hydrolysis of beans (Phaseolus vulgaris) genetically modified to express different phaseolin types. Food Chem. 2008, 106, 1225-1233.
    • (2008) Food Chem , vol.106 , pp. 1225-1233
    • Montoya, C.A.1    Gomez, A.S.2    Lallès, J.P.3    Souffrant, W.B.4    Beebe, S.5    Leterme, P.6
  • 18
    • 17144410327 scopus 로고    scopus 로고
    • Effects of grinding and thermal treatments on hydrolysis susceptibility of a pea protein (Pisum sativum L.)
    • Le Gall, M.; Guéguen, J.; Séve, B.; Quillien, L. Effects of grinding and thermal treatments on hydrolysis susceptibility of a pea protein (Pisum sativum L.). J. Agric. Food Chem. 2005, 53, 3057-3064.
    • (2005) J. Agric. Food Chem , vol.53 , pp. 3057-3064
    • Le Gall, M.1    Guéguen, J.2    Séve, B.3    Quillien, L.4
  • 19
    • 0032126905 scopus 로고    scopus 로고
    • Influence of naturally acid-soluble proteins from beans (Phaseolus vulgaris L.) on in vitro digestibility determination
    • Genovese, M. I.; Lajolo, F. M. Influence of naturally acid-soluble proteins from beans (Phaseolus vulgaris L.) on in vitro digestibility determination. Food Chem. 1998, 62, 315-323.
    • (1998) Food Chem , vol.62 , pp. 315-323
    • Genovese, M.I.1    Lajolo, F.M.2
  • 20
    • 0021060210 scopus 로고
    • Methods of comparing amino acid composition of proteins: Application to undigested proteins in the preruminant calf
    • Guilloteau, P.; Sauvant, D.; Patureau, P. Methods of comparing amino acid composition of proteins: Application to undigested proteins in the preruminant calf. Ann. Nutr. Metab. 1983, 27, 457-469.
    • (1983) Ann. Nutr. Metab , vol.27 , pp. 457-469
    • Guilloteau, P.1    Sauvant, D.2    Patureau, P.3
  • 21
    • 41849137470 scopus 로고    scopus 로고
    • Protein quality test
    • 2nd ed, Aspen Publishers: New York
    • Nielsen, S. S. Protein quality test. Food analysis, 2nd ed.; Aspen Publishers: New York, 1998; pp. 265-279..
    • (1998) Food analysis , pp. 265-279
    • Nielsen, S.S.1
  • 22
    • 0000130569 scopus 로고
    • Multiple range and multiple F-tests
    • Duncan, D. B. Multiple range and multiple F-tests. Biometrics 1955, 11, 1-42.
    • (1955) Biometrics , vol.11 , pp. 1-42
    • Duncan, D.B.1
  • 23
    • 19944409837 scopus 로고    scopus 로고
    • Molecular analysis and physicochemical properties of electrophoretic variants of wild soybean Glycine soja storage proteins
    • Fukuda, T.; Maruyama, N.; Kanazawa, A.; Abe, A.; Shimamoto, Y.; Hiemori, M.; Tsuji, H.; Tanisaka, T.; Utsumi, S. Molecular analysis and physicochemical properties of electrophoretic variants of wild soybean Glycine soja storage proteins. J. Sci. Food Agric. 2005, 53, 3658-3665.
    • (2005) J. Sci. Food Agric , vol.53 , pp. 3658-3665
    • Fukuda, T.1    Maruyama, N.2    Kanazawa, A.3    Abe, A.4    Shimamoto, Y.5    Hiemori, M.6    Tsuji, H.7    Tanisaka, T.8    Utsumi, S.9
  • 24
    • 33745953569 scopus 로고    scopus 로고
    • Comparison of gastric emptying scintigraphy based on the geometric mean of the gastric proportion of the abdominal radioactivity or on the geometric mean of the intragastric radioactivity
    • Salaun, P. Y.; Querellou, S.; Nguyen, J. M.; Bodet-Milin, C.; Carlier, T.; Turzo, A.; Bizais, Y.; Couturier, O. Comparison of gastric emptying scintigraphy based on the geometric mean of the gastric proportion of the abdominal radioactivity or on the geometric mean of the intragastric radioactivity. Nucl. Med. Commun. 2006, 27, 431-437.
    • (2006) Nucl. Med. Commun , vol.27 , pp. 431-437
    • Salaun, P.Y.1    Querellou, S.2    Nguyen, J.M.3    Bodet-Milin, C.4    Carlier, T.5    Turzo, A.6    Bizais, Y.7    Couturier, O.8
  • 25
    • 33748677777 scopus 로고    scopus 로고
    • Effect of lactose on oro-cecal transit in lactose digesters and maldigesters
    • He, T.; Priebe, M. G.; Welling, G. W.; Vonk, R. F. Effect of lactose on oro-cecal transit in lactose digesters and maldigesters. Eur. J. Clin. Invest. 2006, 36, 737-742.
    • (2006) Eur. J. Clin. Invest , vol.36 , pp. 737-742
    • He, T.1    Priebe, M.G.2    Welling, G.W.3    Vonk, R.F.4
  • 26
    • 0029997826 scopus 로고    scopus 로고
    • Conformation, protein-carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin-lactosa complex
    • Banerjee, R.; Das, K.; Ravishankar, R.; Suguna, K.; Surolia, A.; Vijayan, M. Conformation, protein-carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin-lactosa complex. J. Mol. Biol. 1996, 259, 281-296.
    • (1996) J. Mol. Biol , vol.259 , pp. 281-296
    • Banerjee, R.1    Das, K.2    Ravishankar, R.3    Suguna, K.4    Surolia, A.5    Vijayan, M.6
  • 27
    • 84985234327 scopus 로고
    • Isolation and characterization of the major protein from great northern beans (Phaseolus vulgaris)
    • Chang, K. C.; Satterlee, L. D. Isolation and characterization of the major protein from great northern beans (Phaseolus vulgaris). J. Food Sci. 1981, 46, 1368-1373.
    • (1981) J. Food Sci , vol.46 , pp. 1368-1373
    • Chang, K.C.1    Satterlee, L.D.2
  • 28
    • 84985257187 scopus 로고
    • Structure-digestibility relationship of legume 7S proteins
    • Deshpande, S. S.; Damodaran, S. Structure-digestibility relationship of legume 7S proteins. J. Food Sci. 1989, 54, 108-113.
    • (1989) J. Food Sci , vol.54 , pp. 108-113
    • Deshpande, S.S.1    Damodaran, S.2


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