메뉴 건너뛰기




Volumn 70, Issue 3, 2015, Pages 338-343

Growth Impairment Caused by Raw Linseed Consumption: Can Trypsin Inhibitors Be Harmful for Health?

Author keywords

Albumins; Antinutritional factors; Globulins; Linseed; Protein digestibility; Trypsin inhibitors

Indexed keywords

RATTUS;

EID: 84939465623     PISSN: 09219668     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11130-015-0500-y     Document Type: Article
Times cited : (9)

References (32)
  • 2
    • 4644306812 scopus 로고    scopus 로고
    • Isolation and structural characterization of the major protein fraction from NorMan flaxseed (Linum usitatissimum L.)
    • COI: 1:CAS:528:DC%2BD2cXotV2ju74%3D
    • Chung MWY, Lei B, Li-Chan ECY (2005) Isolation and structural characterization of the major protein fraction from NorMan flaxseed (Linum usitatissimum L.). Food Chem 90:271–279. doi:10.1016/j.foodchem.2003.07.038
    • (2005) Food Chem , vol.90 , pp. 271-279
    • Chung, M.W.Y.1    Lei, B.2    Li-Chan, E.C.Y.3
  • 3
    • 0000731532 scopus 로고
    • Comparison of a commercial soybean cultivar and an isoline lacking the Kunitz trypsin-inhibitor - composition, nutritional-value, and effects of heating
    • COI: 1:CAS:528:DyaK3MXotVansw%3D%3D
    • Friedman M, Brandon DL, Bates AH, Hymowitz T (1991) Comparison of a commercial soybean cultivar and an isoline lacking the Kunitz trypsin-inhibitor - composition, nutritional-value, and effects of heating. J Agric Food Chem 39:327–335. doi:10.1021/jf00002a022
    • (1991) J Agric Food Chem , vol.39 , pp. 327-335
    • Friedman, M.1    Brandon, D.L.2    Bates, A.H.3    Hymowitz, T.4
  • 4
    • 0027273062 scopus 로고
    • Flaxseed proteins - a review
    • COI: 1:CAS:528:DyaK3sXmt1Cnu7s%3D
    • Oomah BD, Mazza G (1993) Flaxseed proteins - a review. Food Chem 48:109–114. doi:10.1016/0308-8146(93)90043-F
    • (1993) Food Chem , vol.48 , pp. 109-114
    • Oomah, B.D.1    Mazza, G.2
  • 5
    • 0028997212 scopus 로고
    • Plant storage proteins
    • Shewry PR (1995) Plant storage proteins. Biol Rev 70:375–426
    • (1995) Biol Rev , vol.70 , pp. 375-426
    • Shewry, P.R.1
  • 6
    • 0001442232 scopus 로고
    • The nitrogenous constituents of flaxseed
    • COI: 1:CAS:528:DyaH2MXjt1Cmtw%3D%3D
    • Vassel B, Nesbitt LL (1945) The nitrogenous constituents of flaxseed. J Biol Chem 159:571–584
    • (1945) J Biol Chem , vol.159 , pp. 571-584
    • Vassel, B.1    Nesbitt, L.L.2
  • 7
    • 0023913814 scopus 로고
    • High and low inhibitor soybean meals affect human duodenal proteinase activity differently - in vivo comparison with bovine serum-albumin
    • Holm H, Hanssen LE, Krogdahl A, Florholmen J (1988) High and low inhibitor soybean meals affect human duodenal proteinase activity differently - in vivo comparison with bovine serum-albumin. J Nutr 118:515–520
    • (1988) J Nutr , vol.118 , pp. 515-520
    • Holm, H.1    Hanssen, L.E.2    Krogdahl, A.3    Florholmen, J.4
  • 8
    • 0028309335 scopus 로고
    • Implications of antinutritional components in soybean foods
    • Liener IE (1994) Implications of antinutritional components in soybean foods. Crit Rev Food Sci Nutr 34:31–67. doi:10.1080/10408399409527649
    • (1994) Crit Rev Food Sci Nutr , vol.34 , pp. 31-67
    • Liener, I.E.1
  • 9
    • 0030171564 scopus 로고    scopus 로고
    • Cowpea inhibition of human and bovine protease activities and the effects of processing
    • Nti CA, Plahar WA (1996) Cowpea inhibition of human and bovine protease activities and the effects of processing. Food Control 7:129–133. doi:10.1016/0956-7135(96)00017-5
    • (1996) Food Control , vol.7 , pp. 129-133
    • Nti, C.A.1    Plahar, W.A.2
  • 10
    • 0037013551 scopus 로고    scopus 로고
    • Effects of removal of mucilage and enzyme or sepiolite supplement on the nutrient digestibility and metabolyzable energy of a diet containing linseed in broiler chickens
    • COI: 1:CAS:528:DC%2BD38XktFKgurw%3D
    • Alzueta C, Ortiz LT, Rebole A, Rodriguez ML, Centeno C, Trevino J (2002) Effects of removal of mucilage and enzyme or sepiolite supplement on the nutrient digestibility and metabolyzable energy of a diet containing linseed in broiler chickens. Anim Feed Sci Technol 97:169–181. doi:10.1016/S0377-8401(02)00030-5
    • (2002) Anim Feed Sci Technol , vol.97 , pp. 169-181
    • Alzueta, C.1    Ortiz, L.T.2    Rebole, A.3    Rodriguez, M.L.4    Centeno, C.5    Trevino, J.6
  • 11
    • 85033705291 scopus 로고    scopus 로고
    • Isolation and amino acid sequence of a serine proteinase inhibitor from common flax (Linum usitatissimum) seeds
    • Lorenc-Kubis I, Kowalska JB, Pochroń Zuzło A, Wilusz T (2001) Isolation and amino acid sequence of a serine proteinase inhibitor from common flax (Linum usitatissimum) seeds. Chembiochem 2:41–51. doi:10.1002/1439-7633(20010105)2:1<45::AID-CBIC45>3.0.CO;2-#
    • (2001) Chembiochem , vol.2 , pp. 41-51
    • Lorenc-Kubis, I.1    Kowalska, J.B.2    Pochroń Zuzło, A.3    Wilusz, T.4
  • 12
    • 0000736550 scopus 로고
    • Poor correlation between the levels of proteinase-inhibitors found in seeds of different cultivars of cowpea (Vigna-Unguiculata) and the resistance susceptibility to predation by Callosobruchusmaculatus
    • Xavier-Filho J, Campos FAP, Ary MB, Silva CP, Carvalho MMM, Macedo MLR, Lemos FJA, Grant G (1989) Poor correlation between the levels of proteinase-inhibitors found in seeds of different cultivars of cowpea (Vigna-Unguiculata) and the resistance susceptibility to predation by Callosobruchusmaculatus. J Agric Food Chem 37:1139–1143. doi:10.1021/jf00088a071
    • (1989) J Agric Food Chem , vol.37 , pp. 1139-1143
    • Xavier-Filho, J.1    Campos, F.A.P.2    Ary, M.B.3    Silva, C.P.4    Carvalho, M.M.M.5    Macedo, M.L.R.6    Lemos, F.J.A.7    Grant, G.8
  • 13
    • 33749531916 scopus 로고    scopus 로고
    • The interaction of the 11S globulin-like protein of kiwifruit seeds with pepsin
    • COI: 1:CAS:528:DC%2BD28XhtVOrt7vM
    • Rassam M, Laing WA (2006) The interaction of the 11S globulin-like protein of kiwifruit seeds with pepsin. Plant Sci 171:663–669. doi:10.1016/j.plantsci.2006.06.014
    • (2006) Plant Sci , vol.171 , pp. 663-669
    • Rassam, M.1    Laing, W.A.2
  • 14
    • 0017184389 scopus 로고
    • Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding
    • COI: 1:CAS:528:DyaE28XksVehtrY%3D
    • Bradford MM (1976) Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding. Anal Biochem 72:248–254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 15
    • 0019572737 scopus 로고
    • Specificity of 12 lectins towards oligosaccharides and glycopeptides related to N-glycosylproteins
    • COI: 1:CAS:528:DyaL3MXkvFGhtb0%3D
    • Debray H, Decout D, Strecker G, Spik G, Montreuil J (1981) Specificity of 12 lectins towards oligosaccharides and glycopeptides related to N-glycosylproteins. Eur J Biochem 117:41–55. doi:10.1111/j.1432-1033.1981.tb06300.x
    • (1981) Eur J Biochem , vol.117 , pp. 41-55
    • Debray, H.1    Decout, D.2    Strecker, G.3    Spik, G.4    Montreuil, J.5
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of head of bacteriophage-T4
    • COI: 1:CAS:528:DC%2BD3MXlsFags7s%3D
    • Laemmli UK (1970) Cleavage of structural proteins during assembly of head of bacteriophage-T4. Nature 227:680–685. doi:10.1038/227680a0
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0030912476 scopus 로고    scopus 로고
    • Components of the AIN-93 diets as improvements in the AIN-76A diet
    • COI: 1:CAS:528:DyaK2sXjtVCisbc%3D
    • Reeves PG (1997) Components of the AIN-93 diets as improvements in the AIN-76A diet. J Nutr 127(5, Suppl):838S–841S
    • (1997) J Nutr , vol.127 , pp. 838S-841S
    • Reeves, P.G.1
  • 19
    • 0004500610 scopus 로고
    • The biological value of proteins: further investigation of the balance sheet method
    • COI: 1:CAS:528:DyaA2MXls1GjtQ%3D%3D
    • Chick H, Hutchinson JC, Jackson HM (1935) The biological value of proteins: further investigation of the balance sheet method. Biochem J 29:1702–1711
    • (1935) Biochem J , vol.29 , pp. 1702-1711
    • Chick, H.1    Hutchinson, J.C.2    Jackson, H.M.3
  • 20
    • 0003309726 scopus 로고
    • Nutritional evaluation of protein foods
    • Pellet PR, Young VL (1980) Nutritional evaluation of protein foods. Food Nutr Bull 4:154
    • (1980) Food Nutr Bull , vol.4 , pp. 154
    • Pellet, P.R.1    Young, V.L.2
  • 21
    • 84987277329 scopus 로고
    • In vitro enzymatic-hydrolysis of phaseolin, the major storage protein of Phaseolus vulgaris L
    • Deshpande SS, Nielsen SS (1987) In vitro enzymatic-hydrolysis of phaseolin, the major storage protein of Phaseolus vulgaris L. J Food Sci 52:1326–1329. doi:10.1111/j.1365-2621.1987.tb14074.x
    • (1987) J Food Sci , vol.52 , pp. 1326-1329
    • Deshpande, S.S.1    Nielsen, S.S.2
  • 22
    • 0002788050 scopus 로고
    • In vitro and in vivo studies on the digestibility of the major storage protein of the navy bean (Phaseolusvulgaris)
    • Liener IE, Thompson RM (1980) In vitro and in vivo studies on the digestibility of the major storage protein of the navy bean (Phaseolusvulgaris). Plant Foods Hum Nutr 30:13–25
    • (1980) Plant Foods Hum Nutr , vol.30 , pp. 13-25
    • Liener, I.E.1    Thompson, R.M.2
  • 23
    • 0040714323 scopus 로고    scopus 로고
    • Effect of cooking on the protein digestibility of sorghum
    • COI: 1:CAS:528:DyaK1cXlsV2lsrg%3D
    • Agudelo RA, Alarcon OM, Fliedel G (1998) Effect of cooking on the protein digestibility of sorghum. Arch Latinoam Nutr 48:47–51
    • (1998) Arch Latinoam Nutr , vol.48 , pp. 47-51
    • Agudelo, R.A.1    Alarcon, O.M.2    Fliedel, G.3
  • 24
    • 0036323160 scopus 로고    scopus 로고
    • In vitro digestibility of globulins from cowpea (Vigna unguiculata) and xerophitic algaroba (Prosopis juliflora) seeds by mammalian digestive proteinases: a comparative study
    • Araújo AH, Cardoso PCB, Pereira RA, Lima LM, Oliveira AS, Miranda MRA, Xavier-Filho J, Sales MP (2002) In vitro digestibility of globulins from cowpea (Vigna unguiculata) and xerophitic algaroba (Prosopis juliflora) seeds by mammalian digestive proteinases: a comparative study. Food Chem 78:143–147. doi:10.1016/S0956-7135(03)00021-5
    • (2002) Food Chem , vol.78 , pp. 143-147
    • Araújo, A.H.1    Cardoso, P.C.B.2    Pereira, R.A.3    Lima, L.M.4    Oliveira, A.S.5    Miranda, M.R.A.6    Xavier-Filho, J.7    Sales, M.P.8
  • 25
    • 0242406654 scopus 로고    scopus 로고
    • Comparative digestibility and the inhibition of mammalian digestive enzymes from mature and immature cowpea (Vigna unguiculata (L.) Walp.) seeds
    • Lima LM, Araujo AH, Oliveira AS, Pereira RA, Miranda MRA, Sales MP (2004) Comparative digestibility and the inhibition of mammalian digestive enzymes from mature and immature cowpea (Vigna unguiculata (L.) Walp.) seeds. Food Control 15:107–110. doi:10.1016/S0956-7135(03)00021-5
    • (2004) Food Control , vol.15 , pp. 107-110
    • Lima, L.M.1    Araujo, A.H.2    Oliveira, A.S.3    Pereira, R.A.4    Miranda, M.R.A.5    Sales, M.P.6
  • 26
    • 84984529495 scopus 로고
    • In vitro digestibility of proteins in black gram (Phaseolus mungo) and green gram (Phaseolus radiatus) papads
    • Shashikala M, Prakash J (1995) In vitro digestibility of proteins in black gram (Phaseolus mungo) and green gram (Phaseolus radiatus) papads. Nahrung 39:42–47. doi:10.1002/food.19950390105
    • (1995) Nahrung , vol.39 , pp. 42-47
    • Shashikala, M.1    Prakash, J.2
  • 27
    • 0031007727 scopus 로고    scopus 로고
    • Amino acid composition, available lysine content and in vitro protein digestibility of selected tropical crop seeds
    • COI: 1:STN:280:DyaK2szksFersA%3D%3D
    • Petzke KJ, Ezeagu IE, Proll J, Akinsoyinu AO, Metges CC (1997) Amino acid composition, available lysine content and in vitro protein digestibility of selected tropical crop seeds. Plant Foods Hum Nutr 50:151–162
    • (1997) Plant Foods Hum Nutr , vol.50 , pp. 151-162
    • Petzke, K.J.1    Ezeagu, I.E.2    Proll, J.3    Akinsoyinu, A.O.4    Metges, C.C.5
  • 28
    • 78049309091 scopus 로고    scopus 로고
    • Purification and modes of antifungal action by Vicia faba cv. Egypt trypsin inhibitor
    • COI: 1:CAS:528:DC%2BC3cXhtFChs7nK
    • Fang EF, Hassanien AAE, Wong JH, Bah CSF, Soliman SS, Ng TB (2010) Purification and modes of antifungal action by Vicia faba cv. Egypt trypsin inhibitor. J Agric Food Chem 58:10729–10735. doi:10.1021/jf102277k
    • (2010) J Agric Food Chem , vol.58 , pp. 10729-10735
    • Fang, E.F.1    Hassanien, A.A.E.2    Wong, J.H.3    Bah, C.S.F.4    Soliman, S.S.5    Ng, T.B.6
  • 30
    • 84865125141 scopus 로고    scopus 로고
    • The heat-induced protein aggregate correlated with trypsin inhibitor inactivation in soymilk processing
    • Zhicun X, Yeming C, Caimeng Z, Xiangzhen K, Yufei H (2012) The heat-induced protein aggregate correlated with trypsin inhibitor inactivation in soymilk processing. J Agric Food Chem 60:8012–8019. doi:10.1021/jf3021249
    • (2012) J Agric Food Chem , vol.60 , pp. 8012-8019
    • Zhicun, X.1    Yeming, C.2    Caimeng, Z.3    Xiangzhen, K.4    Yufei, H.5
  • 31
    • 84939463486 scopus 로고
    • The nutritional significance of naturally occurring toxins in plant foodstuffs
    • Liener IE (1985) The nutritional significance of naturally occurring toxins in plant foodstuffs. Toxicon 23:544
    • (1985) Toxicon , vol.23 , pp. 544
    • Liener, I.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.