메뉴 건너뛰기




Volumn 45, Issue 2, 2010, Pages 217-222

The effect of limited hydrolysis with Neutrase and ultrafiltration on the anti-adipogenic activity of soy protein

Author keywords

3T3 L1 cell; Anti adipogenic activity; Limited hydrolysis; Soy protein; Ultrafiltration membrane

Indexed keywords

ADIPOGENIC; ANTI-ADIPOGENIC ACTIVITY; SOY PROTEIN; ULTRA-FILTRATION MEMBRANES; ULTRAFILTRATION MEMBRANE;

EID: 71249110146     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2009.09.010     Document Type: Article
Times cited : (26)

References (33)
  • 1
    • 33645758029 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme derived from soy protein hydrolysate and produced by using membrane reactor
    • Chiang W.D., Tsou M.J., Tsai Z.Y., and Tsai T.C. Angiotensin I-converting enzyme derived from soy protein hydrolysate and produced by using membrane reactor. Food Chem 98 (2006) 725-732
    • (2006) Food Chem , vol.98 , pp. 725-732
    • Chiang, W.D.1    Tsou, M.J.2    Tsai, Z.Y.3    Tsai, T.C.4
  • 2
    • 6944251245 scopus 로고    scopus 로고
    • Soyabean protein hydrolysate prevents the development of hypertension in spontaneously hypertensive rats
    • Yang H.Y., Yang S.C., Chen J.R., Tzeng Y.H., and Han B.C. Soyabean protein hydrolysate prevents the development of hypertension in spontaneously hypertensive rats. Br J Nutr 92 (2004) 507-512
    • (2004) Br J Nutr , vol.92 , pp. 507-512
    • Yang, H.Y.1    Yang, S.C.2    Chen, J.R.3    Tzeng, Y.H.4    Han, B.C.5
  • 3
    • 0034192039 scopus 로고    scopus 로고
    • Soy protein isolate and its hydrolysate reduce body fat of dietary obese rats and genetically obese mice (yellow KK)
    • Aoyama T., Fukui K., Takamatsu K., Hashimoto Y., and Yamamoto T. Soy protein isolate and its hydrolysate reduce body fat of dietary obese rats and genetically obese mice (yellow KK). Nutrition 16 (2000) 349-354
    • (2000) Nutrition , vol.16 , pp. 349-354
    • Aoyama, T.1    Fukui, K.2    Takamatsu, K.3    Hashimoto, Y.4    Yamamoto, T.5
  • 4
    • 0031080696 scopus 로고    scopus 로고
    • Serum cholesterol reduction and cholesterol absorption inhibition in Caco-2 cells by a soyprotein peptic hydrolyzate
    • Nagaoka S., Awano T., Nagata N., Masaoka M., Hori G., and Hashimoto K. Serum cholesterol reduction and cholesterol absorption inhibition in Caco-2 cells by a soyprotein peptic hydrolyzate. Biosci Biotechnol Biochem 61 (1997) 354-356
    • (1997) Biosci Biotechnol Biochem , vol.61 , pp. 354-356
    • Nagaoka, S.1    Awano, T.2    Nagata, N.3    Masaoka, M.4    Hori, G.5    Hashimoto, K.6
  • 5
    • 34548292478 scopus 로고    scopus 로고
    • Calcium-binding ability of soy protein hydrolysates
    • Bao X.L., Song M., Zhang J., Chen Y., and Guo S.T. Calcium-binding ability of soy protein hydrolysates. Chin Chem Lett 18 (2007) 1115-1118
    • (2007) Chin Chem Lett , vol.18 , pp. 1115-1118
    • Bao, X.L.1    Song, M.2    Zhang, J.3    Chen, Y.4    Guo, S.T.5
  • 6
    • 0016442025 scopus 로고
    • Role of glycerol 3-phosphate dehydrogenase in glyceride metabolism. Effect of diet on enzyme activities in chicken liver
    • Harding J.W., Pyeritz E.A., Copeland E.S., and White H.B. Role of glycerol 3-phosphate dehydrogenase in glyceride metabolism. Effect of diet on enzyme activities in chicken liver. Biochem J 146 (1975) 223-229
    • (1975) Biochem J , vol.146 , pp. 223-229
    • Harding, J.W.1    Pyeritz, E.A.2    Copeland, E.S.3    White, H.B.4
  • 7
    • 0016165240 scopus 로고
    • Pathways of glyceride glycerol synthesis
    • Rognstad R., Clark D.G., and Katz J. Pathways of glyceride glycerol synthesis. Biochem J 140 (1974) 249-251
    • (1974) Biochem J , vol.140 , pp. 249-251
    • Rognstad, R.1    Clark, D.G.2    Katz, J.3
  • 8
    • 0026034102 scopus 로고
    • Glycerol 3-phosphate dehydrogenase gene expression in cultured 3T3-L1 adipocytes: regulation by insulin, dexamethasone and dibutyryl cAMP at the level of mRNA abundance, transcription and mRNA stability
    • Bhandari B., Saini K.S., and Miller R.E. Glycerol 3-phosphate dehydrogenase gene expression in cultured 3T3-L1 adipocytes: regulation by insulin, dexamethasone and dibutyryl cAMP at the level of mRNA abundance, transcription and mRNA stability. Mol Cell Endocrinol 76 (1991) 71-77
    • (1991) Mol Cell Endocrinol , vol.76 , pp. 71-77
    • Bhandari, B.1    Saini, K.S.2    Miller, R.E.3
  • 9
    • 0024512680 scopus 로고
    • Regulation of gene expression by insulin in adipose cells: opposite effects on adipsin and glycerophosphate dehydrogenase genes
    • Dani C., Bertrand B., Bardon S., Doglio A., Amri E., and Grimaldi P. Regulation of gene expression by insulin in adipose cells: opposite effects on adipsin and glycerophosphate dehydrogenase genes. Mol Cell Endocrinol 63 (1989) 199-208
    • (1989) Mol Cell Endocrinol , vol.63 , pp. 199-208
    • Dani, C.1    Bertrand, B.2    Bardon, S.3    Doglio, A.4    Amri, E.5    Grimaldi, P.6
  • 11
    • 0004647422 scopus 로고
    • A study of the adipose conversion of suspended 3T3 cells by using glycerophosphate dehydrogenase as a differentiation marker
    • Pairault F., and Green H. A study of the adipose conversion of suspended 3T3 cells by using glycerophosphate dehydrogenase as a differentiation marker. Proc Natl Acad Sci U S A 76 (1979) 5138-5142
    • (1979) Proc Natl Acad Sci U S A , vol.76 , pp. 5138-5142
    • Pairault, F.1    Green, H.2
  • 14
    • 0018276872 scopus 로고
    • Development of hormone receptors and hormonal responsiveness in vitro. Insulin receptors and insulin sensitivity in the preadipocyte and adipocyte forms of 3T3-L1 cells
    • Rubin C.S., Hirsch A., Fung C., and Rosen O.M. Development of hormone receptors and hormonal responsiveness in vitro. Insulin receptors and insulin sensitivity in the preadipocyte and adipocyte forms of 3T3-L1 cells. J Biol Chem 253 (1978) 7570-7578
    • (1978) J Biol Chem , vol.253 , pp. 7570-7578
    • Rubin, C.S.1    Hirsch, A.2    Fung, C.3    Rosen, O.M.4
  • 15
    • 0033213631 scopus 로고    scopus 로고
    • PPAR gamma is required for the differentiation of adipose tissue in vivo and in vitro
    • Rosen E.D., Sarraf P., Troy A.E., Bradwin G., Moore K., Milstone D.S., et al. PPAR gamma is required for the differentiation of adipose tissue in vivo and in vitro. Mol Cell 4 (1999) 611-617
    • (1999) Mol Cell , vol.4 , pp. 611-617
    • Rosen, E.D.1    Sarraf, P.2    Troy, A.E.3    Bradwin, G.4    Moore, K.5    Milstone, D.S.6
  • 17
    • 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., and Catignani G.L. Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins. J Dairy Sci 66 (1983) 1219-1227
    • (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
  • 18
    • 0016693548 scopus 로고
    • An established preadipose cell line and its differentiation in culture. II. Factors affecting the adipose conversion
    • Green H., and Kehinde O. An established preadipose cell line and its differentiation in culture. II. Factors affecting the adipose conversion. Cell 5 (1975) 19-27
    • (1975) Cell , vol.5 , pp. 19-27
    • Green, H.1    Kehinde, O.2
  • 19
    • 0018800219 scopus 로고
    • Participation of one isozyme of cytosolic glycerophosphate dehydrogenase in the adipose conversion of 3T3 cells
    • Wise L.S., and Green H. Participation of one isozyme of cytosolic glycerophosphate dehydrogenase in the adipose conversion of 3T3 cells. J Biol Chem 254 (1979) 273-275
    • (1979) J Biol Chem , vol.254 , pp. 273-275
    • Wise, L.S.1    Green, H.2
  • 20
    • 0036219595 scopus 로고    scopus 로고
    • Characterization of inhibition and stability of soy-protein-derived angiotensin I-converting enzyme inhibitory peptides
    • Wu J., and Ding X. Characterization of inhibition and stability of soy-protein-derived angiotensin I-converting enzyme inhibitory peptides. Food Res Int 35 (2002) 367-375
    • (2002) Food Res Int , vol.35 , pp. 367-375
    • Wu, J.1    Ding, X.2
  • 21
    • 12344251713 scopus 로고    scopus 로고
    • Effect of limited hydrolysis of sunflower protein on the interactions with polysaccharides in foams
    • Martinez K.D., Baeza R.I., Millan F., and Pilosof A.M.R. Effect of limited hydrolysis of sunflower protein on the interactions with polysaccharides in foams. Food Hydrocolloids 19 (2005) 361-369
    • (2005) Food Hydrocolloids , vol.19 , pp. 361-369
    • Martinez, K.D.1    Baeza, R.I.2    Millan, F.3    Pilosof, A.M.R.4
  • 22
    • 0036314589 scopus 로고    scopus 로고
    • Foaming and emulsifying properties of fractions of gluten peptides obtained by limited enzymatic hydrolysis and ultrafiltration
    • Popineau Y., Huchet B., Larré C., and Bérot S. Foaming and emulsifying properties of fractions of gluten peptides obtained by limited enzymatic hydrolysis and ultrafiltration. J Cereal Sci 35 (2002) 327-335
    • (2002) J Cereal Sci , vol.35 , pp. 327-335
    • Popineau, Y.1    Huchet, B.2    Larré, C.3    Bérot, S.4
  • 23
    • 0034873949 scopus 로고    scopus 로고
    • Rheological characterization of a gel formed during extensive enzymatic hydrolysis
    • Doucet D., Gauthier S.F., and Foegeding E.A. Rheological characterization of a gel formed during extensive enzymatic hydrolysis. J Food Sci 66 (2001) 711-715
    • (2001) J Food Sci , vol.66 , pp. 711-715
    • Doucet, D.1    Gauthier, S.F.2    Foegeding, E.A.3
  • 24
    • 0032049440 scopus 로고    scopus 로고
    • Gelation of hydrolysates of a whey protein isolate induced by heat, protease, salts and acid
    • Ju Z.Y., and Kilara A. Gelation of hydrolysates of a whey protein isolate induced by heat, protease, salts and acid. Int Dairy J 8 (1998) 303-309
    • (1998) Int Dairy J , vol.8 , pp. 303-309
    • Ju, Z.Y.1    Kilara, A.2
  • 25
    • 33748431810 scopus 로고    scopus 로고
    • Antioxidant activity of zein hydrolysates in a liposome system and the possible mode of action
    • Kong B., and Xiong Y.L. Antioxidant activity of zein hydrolysates in a liposome system and the possible mode of action. J Agric Food Chem 54 (2006) 6059-6068
    • (2006) J Agric Food Chem , vol.54 , pp. 6059-6068
    • Kong, B.1    Xiong, Y.L.2
  • 26
    • 33646085799 scopus 로고    scopus 로고
    • Antioxidant and free radical-scavenging activities of wheat germ protein hydrolysates (WGPH) prepared with alcalase
    • Zhu K., Zhou H., and Qian H. Antioxidant and free radical-scavenging activities of wheat germ protein hydrolysates (WGPH) prepared with alcalase. Process Biochem 41 (2006) 1296-1302
    • (2006) Process Biochem , vol.41 , pp. 1296-1302
    • Zhu, K.1    Zhou, H.2    Qian, H.3
  • 27
    • 67949123116 scopus 로고    scopus 로고
    • Limited enzymatic hydrolysis of soy protein enhances cholesterol absorption inhibition in Caco-2 cells
    • Tsou M.J., Kao F.J., Hhuang J.B., and Chiang W.D. Limited enzymatic hydrolysis of soy protein enhances cholesterol absorption inhibition in Caco-2 cells. Taiwanese J Agri Chem Food Sci 47 (2009) 1-8
    • (2009) Taiwanese J Agri Chem Food Sci , vol.47 , pp. 1-8
    • Tsou, M.J.1    Kao, F.J.2    Hhuang, J.B.3    Chiang, W.D.4
  • 28
    • 46249133973 scopus 로고    scopus 로고
    • Production of angiotensin I-converting enzyme inhibitor derived from egg white protein hydrolysates using a membrane reactor
    • Chiang W.D., Tsou M.J., Weng C.H., and Tsai T.C. Production of angiotensin I-converting enzyme inhibitor derived from egg white protein hydrolysates using a membrane reactor. J Food Drug Anal 16 (2008) 54-60
    • (2008) J Food Drug Anal , vol.16 , pp. 54-60
    • Chiang, W.D.1    Tsou, M.J.2    Weng, C.H.3    Tsai, T.C.4
  • 29
    • 0033860508 scopus 로고    scopus 로고
    • Classification and antihypertensive activity of angiotensin I-converting enzyme inhibitory peptides derived from food protein
    • Fujita H., Yokoyama K., and Yoshikawa M. Classification and antihypertensive activity of angiotensin I-converting enzyme inhibitory peptides derived from food protein. J Food Sci 65 (2000) 564-569
    • (2000) J Food Sci , vol.65 , pp. 564-569
    • Fujita, H.1    Yokoyama, K.2    Yoshikawa, M.3
  • 30
    • 0023232644 scopus 로고
    • Effect of peptide chain length on absorption of egg protein hydrolysates in the normal human jejunum
    • Grimble G.K., Rees R.G., Keohane P.P., Cartwright T., Desreumaux M., and Silk D.G. Effect of peptide chain length on absorption of egg protein hydrolysates in the normal human jejunum. Gastroenterology 92 (1987) 136-142
    • (1987) Gastroenterology , vol.92 , pp. 136-142
    • Grimble, G.K.1    Rees, R.G.2    Keohane, P.P.3    Cartwright, T.4    Desreumaux, M.5    Silk, D.G.6
  • 31
    • 0031821520 scopus 로고    scopus 로고
    • Understanding adipocyte differentiation
    • Gregoire F.M., Sams C.M., and Sul H.S. Understanding adipocyte differentiation. Physiol Rev 78 (1998) 783-809
    • (1998) Physiol Rev , vol.78 , pp. 783-809
    • Gregoire, F.M.1    Sams, C.M.2    Sul, H.S.3
  • 32
    • 0028878375 scopus 로고
    • Cascade regulation of terminal adipocyte differentiation by three members of the C/EBP family of leucine zipper proteins
    • Yeh W.C., Cao Z., Classon M., and McKnight S.L. Cascade regulation of terminal adipocyte differentiation by three members of the C/EBP family of leucine zipper proteins. Genes Dev 9 (1995) 168-181
    • (1995) Genes Dev , vol.9 , pp. 168-181
    • Yeh, W.C.1    Cao, Z.2    Classon, M.3    McKnight, S.L.4
  • 33
    • 0033200389 scopus 로고    scopus 로고
    • Activation and centromeric localization of CCAAT/enhancer-binding proteins during the mitotic clonal expansion of adipocyte differentiation
    • Tang Q.Q., and Lane M.D. Activation and centromeric localization of CCAAT/enhancer-binding proteins during the mitotic clonal expansion of adipocyte differentiation. Genes Dev 13 (1999) 2231-2241
    • (1999) Genes Dev , vol.13 , pp. 2231-2241
    • Tang, Q.Q.1    Lane, M.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.