메뉴 건너뛰기




Volumn 33, Issue 3, 2014, Pages 521-537

Co-suppression of synthesis of major α-kafirin sub-class together with γ-kafirin-1 and γ-kafirin-2 required for substantially improved protein digestibility in transgenic sorghum

Author keywords

Biofortified; Gamma kafirin; Protein bodies; Protein digestibility; Sorghum; Transgenic

Indexed keywords

KAFIRIN PROTEIN, SORGHUM BICOLOR; VEGETABLE PROTEIN;

EID: 84893980995     PISSN: 07217714     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00299-013-1556-5     Document Type: Article
Times cited : (45)

References (64)
  • 1
    • 0003497429 scopus 로고    scopus 로고
    • AACC International10th edn., St Paul: American Association of Cereal Chemists
    • AACC International (2000) Approved methods of AACC, 10th edn. American Association of Cereal Chemists, St Paul.
    • (2000) Approved Methods of AACC
  • 3
    • 0035989811 scopus 로고    scopus 로고
    • Analysis of the aspartic acid metabolic pathway using mutant genes
    • Azevedo RA (2002) Analysis of the aspartic acid metabolic pathway using mutant genes. Amino Acids 22: 217-230.
    • (2002) Amino Acids , vol.22 , pp. 217-230
    • Azevedo, R.A.1
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0021421924 scopus 로고
    • Interaction of proteins with sorghum tannin: mechanism, specificity and significance
    • Butler LG, Riedl DJ, Lebryk D, Blytt H (1984) Interaction of proteins with sorghum tannin: mechanism, specificity and significance. J Am Oil Chem Soc 61: 916-920.
    • (1984) J Am Oil Chem Soc , vol.61 , pp. 916-920
    • Butler, L.G.1    Riedl, D.J.2    Lebryk, D.3    Blytt, H.4
  • 9
    • 80052575506 scopus 로고    scopus 로고
    • Transgenic sorghum with altered kafirin synthesis: kafirin solubility, polymerization, and protein digestion
    • Da Silva LS, Taylor J, Taylor JR (2011a) Transgenic sorghum with altered kafirin synthesis: kafirin solubility, polymerization, and protein digestion. J Agric Food Chem 59: 9265-9270.
    • (2011) J Agric Food Chem , vol.59 , pp. 9265-9270
    • Da Silva, L.S.1    Taylor, J.2    Taylor, J.R.3
  • 10
    • 79960736532 scopus 로고    scopus 로고
    • Effect of suppressing the synthesis of different kafirin sub-classes on grain endosperm texture, protein body structure and protein nutritional quality in improved sorghum lines
    • Da Silva LS, Jung R, Zhao Z, Glassman K, Taylor J, Taylor J (2011b) Effect of suppressing the synthesis of different kafirin sub-classes on grain endosperm texture, protein body structure and protein nutritional quality in improved sorghum lines. J Cereal Sci 54: 160-167.
    • (2011) J Cereal Sci , vol.54 , pp. 160-167
    • Da Silva, L.S.1    Jung, R.2    Zhao, Z.3    Glassman, K.4    Taylor, J.5    Taylor, J.6
  • 12
    • 0042376089 scopus 로고    scopus 로고
    • Factors affecting sorghum protein digestibility
    • Duodu K, Taylor J, Belton P, Hamaker B (2003) Factors affecting sorghum protein digestibility. J Cereal Sci 38: 117-131.
    • (2003) J Cereal Sci , vol.38 , pp. 117-131
    • Duodu, K.1    Taylor, J.2    Belton, P.3    Hamaker, B.4
  • 13
    • 0001141868 scopus 로고    scopus 로고
    • Characterisation of sorghum kafirins in relation to their cross-linking behaviour
    • El Nour I, Peruffo A, Curioni A (1998) Characterisation of sorghum kafirins in relation to their cross-linking behaviour. J Cereal Sci 28: 197-207.
    • (1998) J Cereal Sci , vol.28 , pp. 197-207
    • El Nour, I.1    Peruffo, A.2    Curioni, A.3
  • 14
    • 0000952749 scopus 로고    scopus 로고
    • Condensed tannins are only partially responsible for variations in nutrient digestibilities of sorghum grain cultivars
    • Elkin RG, Freed MB, Hamaker BR, Zhang Y, Parsons CM (1996) Condensed tannins are only partially responsible for variations in nutrient digestibilities of sorghum grain cultivars. J Agric Food Chem 44: 848-853.
    • (1996) J Agric Food Chem , vol.44 , pp. 848-853
    • Elkin, R.G.1    Freed, M.B.2    Hamaker, B.R.3    Zhang, Y.4    Parsons, C.M.5
  • 15
    • 61449244749 scopus 로고    scopus 로고
    • Properties of heat-treated sorghum and maize meal and their prolamin proteins
    • Emmambux MN, Taylor JR (2009) Properties of heat-treated sorghum and maize meal and their prolamin proteins. J Agric Food Chem 57: 1045-1050.
    • (2009) J Agric Food Chem , vol.57 , pp. 1045-1050
    • Emmambux, M.N.1    Taylor, J.R.2
  • 16
    • 14644390873 scopus 로고    scopus 로고
    • Isolation and characterization of enzymes involved in lysine catabolism from sorghum seeds
    • Fornazier RF, Gaziola SA, Helm CV, Lea PJ, Azevedo RA (2005) Isolation and characterization of enzymes involved in lysine catabolism from sorghum seeds. J Agric Food Chem 53: 1791-1798.
    • (2005) J Agric Food Chem , vol.53 , pp. 1791-1798
    • Fornazier, R.F.1    Gaziola, S.A.2    Helm, C.V.3    Lea, P.J.4    Azevedo, R.A.5
  • 19
    • 77953189093 scopus 로고    scopus 로고
    • Biolistic mediated sorghum (Sorghum bicolor L. Moench) transformation via mannose and bialaphos based selection systems
    • Grootboom AW, Mkhonza N, O'Kennedy M, Chakauya E, Kunert K, Chikwamba R (2010) Biolistic mediated sorghum (Sorghum bicolor L. Moench) transformation via mannose and bialaphos based selection systems. Int J Bot 6(2): 89-94.
    • (2010) Int J Bot , vol.6 , Issue.2 , pp. 89-94
    • Grootboom, A.W.1    Mkhonza, N.2    O'Kennedy, M.3    Chakauya, E.4    Kunert, K.5    Chikwamba, R.6
  • 22
    • 0001680465 scopus 로고
    • Effect of cooking on the protein profiles and in vitro digestibility of sorghum and maize
    • Hamaker BR, Kirleis AW, Mertz ET, Axtell JD (1986) Effect of cooking on the protein profiles and in vitro digestibility of sorghum and maize. J Agric Food Chem 34: 647-649.
    • (1986) J Agric Food Chem , vol.34 , pp. 647-649
    • Hamaker, B.R.1    Kirleis, A.W.2    Mertz, E.T.3    Axtell, J.D.4
  • 23
    • 0029189864 scopus 로고
    • Efficient procedure for extracting maize and sorghum kernel proteins reveals higher prolamin contents than the conventional method
    • Hamaker B, Mohamed A, Habben J, Huang C, Larkins B (1995) Efficient procedure for extracting maize and sorghum kernel proteins reveals higher prolamin contents than the conventional method. Cereal Chem 72: 583-588.
    • (1995) Cereal Chem , vol.72 , pp. 583-588
    • Hamaker, B.1    Mohamed, A.2    Habben, J.3    Huang, C.4    Larkins, B.5
  • 24
    • 0001390168 scopus 로고
    • Influence of tannin content on preharvest seed germination in sorghum
    • Harris HB, Burns RE (1970) Influence of tannin content on preharvest seed germination in sorghum. Agronomy Journal 62(6): 835-836.
    • (1970) Agronomy Journal , vol.62 , Issue.6 , pp. 835-836
    • Harris, H.B.1    Burns, R.E.2
  • 25
    • 79952763940 scopus 로고    scopus 로고
    • The importance of dietary protein in human health: combating protein deficiency in sub-Saharan Africa through transgenic biofortified sorghum
    • Henley E, Taylor J, Obukosia S (2010) The importance of dietary protein in human health: combating protein deficiency in sub-Saharan Africa through transgenic biofortified sorghum. Adv Food Nutr Res 60: 21-52.
    • (2010) Adv Food Nutr Res , vol.60 , pp. 21-52
    • Henley, E.1    Taylor, J.2    Obukosia, S.3
  • 28
    • 84893947273 scopus 로고    scopus 로고
    • ICRISAT, Accessed November 2011
    • ICRISAT (2011) ICRISAT Mandate Crops: Sorghum. www. icrisat. org. Accessed November 2011.
    • (2011) ICRISAT Mandate Crops: Sorghum
  • 30
    • 0030844149 scopus 로고    scopus 로고
    • Analysis of a C4 maize pyruvate, orthophosphate dikinase expressed in C3 transgenic Arabidopsis plants
    • Ishimaru K, Ichikawa H, Matsuoka M, Ohsugi R (1997) Analysis of a C4 maize pyruvate, orthophosphate dikinase expressed in C3 transgenic Arabidopsis plants. Plant Sci 129: 57-64.
    • (1997) Plant Sci , vol.129 , pp. 57-64
    • Ishimaru, K.1    Ichikawa, H.2    Matsuoka, M.3    Ohsugi, R.4
  • 34
    • 0001110107 scopus 로고
    • In vitro protein polymerization by quinones or free radicals generated by plant or fungal oxidative enzymes
    • Leatham GF, King V, Stahmann MA (1980) In vitro protein polymerization by quinones or free radicals generated by plant or fungal oxidative enzymes. Phytopathology 70: 1134-1140.
    • (1980) Phytopathology , vol.70 , pp. 1134-1140
    • Leatham, G.F.1    King, V.2    Stahmann, M.A.3
  • 36
    • 0001326044 scopus 로고
    • Effects of surfactants, pH and certain cations on precipitation of proteins by tannins
    • Martin MM, Rocholm DC, Martin JS (1985) Effects of surfactants, pH and certain cations on precipitation of proteins by tannins. J Chem Ecol 11: 485-494.
    • (1985) J Chem Ecol , vol.11 , pp. 485-494
    • Martin, M.M.1    Rocholm, D.C.2    Martin, J.S.3
  • 38
    • 0344401411 scopus 로고
    • Evaluation of methods for tannin analysis in sorghum grain
    • Maxson E, Rooney L (1972) Evaluation of methods for tannin analysis in sorghum grain. Cereal Chem 49: 719-727.
    • (1972) Cereal Chem , vol.49 , pp. 719-727
    • Maxson, E.1    Rooney, L.2
  • 39
    • 0039287356 scopus 로고
    • Agriculture, the island empire
    • Mayer A, Mayer J (1974) Agriculture, the island empire. Daedalus 103(3): 83-95.
    • (1974) Daedalus , vol.103 , Issue.3 , pp. 83-95
    • Mayer, A.1    Mayer, J.2
  • 40
    • 0018650111 scopus 로고
    • Differential fixation of poly (l-arginine) and poly (l-lysine) by tannic acid and its application to the fixation of collagen in electron microscopy
    • Meek KM, Weiss JB (1979) Differential fixation of poly (l-arginine) and poly (l-lysine) by tannic acid and its application to the fixation of collagen in electron microscopy. Biochimica et Biophysica Acta 587: 112-120.
    • (1979) Biochimica Et Biophysica Acta , vol.587 , pp. 112-120
    • Meek, K.M.1    Weiss, J.B.2
  • 43
    • 0018814870 scopus 로고
    • Chemical composition of different varieties of grain sorghum
    • Neucere NJ, Sumrell G (1980) Chemical composition of different varieties of grain sorghum. J Agric Food Chem 28(1): 19-21.
    • (1980) J Agric Food Chem , vol.28 , Issue.1 , pp. 19-21
    • Neucere, N.J.1    Sumrell, G.2
  • 44
    • 2442430500 scopus 로고    scopus 로고
    • Pearl millet transformation system using the positive selectable marker gene phosphomannose isomerase
    • O'Kennedy M, Burger J, Botha F (2004a) Pearl millet transformation system using the positive selectable marker gene phosphomannose isomerase. Plant Cell Rep 22: 684-690.
    • (2004) Plant Cell Rep , vol.22 , pp. 684-690
    • O'Kennedy, M.1    Burger, J.2    Botha, F.3
  • 45
    • 11244342350 scopus 로고    scopus 로고
    • Improved regeneration efficiency of a pearl millet (Pennisetum glaucum [L.] R. Br.) breeding line
    • O'Kennedy M, Smith G, Botha F (2004b) Improved regeneration efficiency of a pearl millet (Pennisetum glaucum [L.] R. Br.) breeding line. S Afr J Bot 70(4): 502-508.
    • (2004) S Afr J Bot , vol.70 , Issue.4 , pp. 502-508
    • O'Kennedy, M.1    Smith, G.2    Botha, F.3
  • 47
    • 0001450466 scopus 로고
    • Resistance of Sorghum alpha, beta and. gamma-Kafirins to Pepsin Digestion
    • Oria MP, Hamaker BR, Shull JM (1995a) Resistance of Sorghum alpha, beta and. gamma-Kafirins to Pepsin Digestion. J Agric Food Chem 43: 2148-2153.
    • (1995) J Agric Food Chem , vol.43 , pp. 2148-2153
    • Oria, M.P.1    Hamaker, B.R.2    Shull, J.M.3
  • 48
    • 0002884203 scopus 로고
    • In vitro protein digestibility of developing and mature sorghum grain in relation to α-, β-, and γ-kafirin disulfide crosslinking
    • Oria M, Hamaker B, Schull J (1995b) In vitro protein digestibility of developing and mature sorghum grain in relation to α-, β-, and γ-kafirin disulfide crosslinking. J Cereal Sci 22: 85-93.
    • (1995) J Cereal Sci , vol.22 , pp. 85-93
    • Oria, M.1    Hamaker, B.2    Schull, J.3
  • 49
    • 0034625086 scopus 로고    scopus 로고
    • A highly digestible sorghum mutant cultivar exhibits a unique folded structure of endosperm protein bodies
    • Oria MP, Hamaker BR, Axtell JD, Huang C (2000) A highly digestible sorghum mutant cultivar exhibits a unique folded structure of endosperm protein bodies. Proc Natl Acad Sci USA 97: 5060-5070.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5060-5070
    • Oria, M.P.1    Hamaker, B.R.2    Axtell, J.D.3    Huang, C.4
  • 50
    • 0026305374 scopus 로고
    • Variation in mammalian physiological responses to a condensed tannin and its ecological implications
    • Robins CT, Hagerman AE, Austin PJ, McAthur C, Hanley TA (1991) Variation in mammalian physiological responses to a condensed tannin and its ecological implications. J Mammal 72: 480-486.
    • (1991) J Mammal , vol.72 , pp. 480-486
    • Robins, C.T.1    Hagerman, A.E.2    Austin, P.J.3    McAthur, C.4    Hanley, T.A.5
  • 51
    • 0004707741 scopus 로고
    • Effects of cooking and treatment with sodium bisulfite on in vitro protein digestibility and microstructure of sorghum flour
    • Rom D, Shull J, Chandrashekar A, Kirleis A (1992) Effects of cooking and treatment with sodium bisulfite on in vitro protein digestibility and microstructure of sorghum flour. Cereal Chem 69: 178-181.
    • (1992) Cereal Chem , vol.69 , pp. 178-181
    • Rom, D.1    Shull, J.2    Chandrashekar, A.3    Kirleis, A.4
  • 53
    • 3543028757 scopus 로고
    • Genetic variability of alcohol-soluble storage proteins in high-lysine sorghums
    • Sastry LV, Paulis JW, Cobb LA, Wall JS, Axtell JD (1986) Genetic variability of alcohol-soluble storage proteins in high-lysine sorghums. J Agric Food Chem 34: 1061-1067.
    • (1986) J Agric Food Chem , vol.34 , pp. 1061-1067
    • Sastry, L.V.1    Paulis, J.W.2    Cobb, L.A.3    Wall, J.S.4    Axtell, J.D.5
  • 54
    • 2342620174 scopus 로고    scopus 로고
    • The major seed storage proteins of spelt wheat, sorghum, millets and pseudocereals
    • In: Belton PS, Taylor JRN (eds), Springer
    • Shewry PR (2002) The major seed storage proteins of spelt wheat, sorghum, millets and pseudocereals. In: Belton PS, Taylor JRN (eds) Pseudocereals and less common cereals. Springer, pp 1-24.
    • (2002) Pseudocereals and less common cereals , pp. 1-24
    • Shewry, P.R.1
  • 55
    • 35448942767 scopus 로고    scopus 로고
    • Improving the protein content and composition of cereal grain
    • Shewry PR (2007) Improving the protein content and composition of cereal grain. J Cereal Sci 46: 239-250.
    • (2007) J Cereal Sci , vol.46 , pp. 239-250
    • Shewry, P.R.1
  • 56
    • 0001778638 scopus 로고
    • Purification and immunocytochemical localization of kafirins in Sorghum bicolor (L. Moench) endosperm
    • Shull JM, Watterson JJ, Kirleis A (1992) Purification and immunocytochemical localization of kafirins in Sorghum bicolor (L. Moench) endosperm. Protoplasma 171: 64-74.
    • (1992) Protoplasma , vol.171 , pp. 64-74
    • Shull, J.M.1    Watterson, J.J.2    Kirleis, A.3
  • 57
    • 79952746012 scopus 로고    scopus 로고
    • Protein biofortified sorghum: effect of processing into traditional African foods on their protein quality
    • Taylor J, Taylor JR (2011) Protein biofortified sorghum: effect of processing into traditional African foods on their protein quality. J Agric Food Chem 59: 2386-2392.
    • (2011) J Agric Food Chem , vol.59 , pp. 2386-2392
    • Taylor, J.1    Taylor, J.R.2
  • 58
    • 33645801400 scopus 로고    scopus 로고
    • A novel modified endosperm texture in a mutant high-protein digestibility/high-lysine grain sorghum (Sorghum bicolor (L.) Moench)
    • Tesso T, Ejeta G, Chandrashekar A, Huang C, Tandjung A, Lewamy M, Axtell JD, Hamaker BR (2006) A novel modified endosperm texture in a mutant high-protein digestibility/high-lysine grain sorghum (Sorghum bicolor (L.) Moench). Cereal Chem 83: 194-201.
    • (2006) Cereal Chem , vol.83 , pp. 194-201
    • Tesso, T.1    Ejeta, G.2    Chandrashekar, A.3    Huang, C.4    Tandjung, A.5    Lewamy, M.6    Axtell, J.D.7    Hamaker, B.R.8
  • 59
    • 56849083275 scopus 로고    scopus 로고
    • Sorghum protein digestibility is affected by dosage of mutant alleles in endosperm cells
    • Tesso T, Hamaker B, Ejeta G (2008) Sorghum protein digestibility is affected by dosage of mutant alleles in endosperm cells. Plant Breeding 127: 579-586.
    • (2008) Plant Breeding , vol.127 , pp. 579-586
    • Tesso, T.1    Hamaker, B.2    Ejeta, G.3
  • 60
    • 34249831354 scopus 로고
    • Osmotic treatment enhances particle bombardment-mediated transient and stable transformation of maize
    • Vain P, McMullen MD, Finer JJ (1993) Osmotic treatment enhances particle bombardment-mediated transient and stable transformation of maize. Plant Cell Rep 12: 84-88.
    • (1993) Plant Cell Rep , vol.12 , pp. 84-88
    • Vain, P.1    McMullen, M.D.2    Finer, J.J.3
  • 61
    • 0004639050 scopus 로고
    • Quantitation of α-, β-, and γ-kafirins in vitreous and opaque endosperm of Sorghum bicolor
    • Watterson J, Shull J, Kirleis A (1993) Quantitation of α-, β-, and γ-kafirins in vitreous and opaque endosperm of Sorghum bicolor. Cereal Chem 70: 452-457.
    • (1993) Cereal Chem , vol.70 , pp. 452-457
    • Watterson, J.1    Shull, J.2    Kirleis, A.3
  • 62
    • 0031664235 scopus 로고    scopus 로고
    • Discovery of grain sorghum germ plasm with high uncooked and cooked in vitro protein digestibilities
    • Weaver CA, Hamaker BR, Axtell JD (1998) Discovery of grain sorghum germ plasm with high uncooked and cooked in vitro protein digestibilities. Cereal Chem 75: 665-670.
    • (1998) Cereal Chem , vol.75 , pp. 665-670
    • Weaver, C.A.1    Hamaker, B.R.2    Axtell, J.D.3
  • 63
    • 77955604886 scopus 로고    scopus 로고
    • γ-Zeins are essential for endosperm modification in quality protein maize
    • Wu Y, Holding DR, Messing J (2010) γ-Zeins are essential for endosperm modification in quality protein maize. Proc Natl Acad Sci USA 107: 12810-12815.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 12810-12815
    • Wu, Y.1    Holding, D.R.2    Messing, J.3
  • 64
    • 75549087906 scopus 로고    scopus 로고
    • The Africa biofortified sorghum project-applying biotechnology to develop nutritionally improved sorghum for Africa
    • In: Xu Z, Li J, Xue Y, Yang W (eds), Springer
    • Zhao Z (2007) The Africa biofortified sorghum project-applying biotechnology to develop nutritionally improved sorghum for Africa. In: Xu Z, Li J, Xue Y, Yang W (eds) Biotechnology and sustainable agriculture 2006 and beyond. Springer, pp 273-277.
    • (2007) Biotechnology and sustainable agriculture 2006 and beyond , pp. 273-277
    • Zhao, Z.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.