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HMW glutenin

Loponen, J., Mikola, M., Katina, K., Sontag-Strohm, T., Salovaara, H. 2004. Degradation of HMW glutenins during wheat sourdough fermentations. Cereal Chem 81 87-93. [Pg.313]

Halford, N.G., Field, J.M., Blair, H., Urwin, P., Moore, K., Robert, L., Thompson, R., Havell, R.B., Tatham, A.S., and Shewry, P.R. (1992). Analysis of the HMW glutenin subunits encoded by chromosome lA of bread wheat (Tritkum aestimm L.) indicates quantitative effects on grain quaUty. Theor. Appl. Genet., 83, 373-378. [Pg.93]

Payne, P.I., Nightingale, M.A., Krattinger, A.F., and Holt, L.M. (1987). The relationship between HMW glutenin subunit composition and the bread-making quality of British grown... [Pg.93]

Vawser, M.J. and Cornish, G.B. (2004). Over-expression of HMW glutenin subunit Glu-Bl lx in hexaploid wheat varieties (Triticum aestivumh.). Aust. J. Agric. ScL, 55, 577-588. [Pg.93]

Figure 20.7. Structure of HMW glutenin subunit showing (a) branching (b) spiral structure by Atomic Force Microscopy (AFM). (From Humphries et al. (2000), Cereal Chem. 77, 107-110.)... Figure 20.7. Structure of HMW glutenin subunit showing (a) branching (b) spiral structure by Atomic Force Microscopy (AFM). (From Humphries et al. (2000), Cereal Chem. 77, 107-110.)...
Figure 13.10 SDS-PAGE of seed storage proteins of T. aestivum L., cv S. ranozreika 2 and their mutant forms. Lane 1- control of T. aestivum, 2,4,5, 6, and 7 are lanes of mutant forms type sphaerococcum. The HMW-glutenin subunits are with high weight (more than 160,000), and well separated from other prolamins [13]. Figure 13.10 SDS-PAGE of seed storage proteins of T. aestivum L., cv S. ranozreika 2 and their mutant forms. Lane 1- control of T. aestivum, 2,4,5, 6, and 7 are lanes of mutant forms type sphaerococcum. The HMW-glutenin subunits are with high weight (more than 160,000), and well separated from other prolamins [13].
Figure 13.11 SDS-PAGE of polymeric protein (after reduction to subunits). Group A HMW glutenin subunits showing x- and y-type subunits. Group B-, C-, D- LMW glutenin subunits. Arrow indicates subunit D [41]. Figure 13.11 SDS-PAGE of polymeric protein (after reduction to subunits). Group A HMW glutenin subunits showing x- and y-type subunits. Group B-, C-, D- LMW glutenin subunits. Arrow indicates subunit D [41].
Halford, N.G. et al. Analysis of HMW glutenin subunits encoded by chromosome lA of bread wheat (Triticum aestivum L.) indicates quantitative effects on grain quaUty. TAG Theor. Appl. Genet. 83(3) 373-378, January 1992. [Pg.98]

Gupta, R. B., E MacRitchie, K. W. Shepherd, and R Ellison. 1991. Relative contributions of LMW and HMW glutenin subunits to dough strength and dough stickiness of bread wheat. In Gluten proteins 1990, ed. W. Bushuk and R. Tkachuk, 71-80. St. Paul, MN American Association of Cereal Chemists. [Pg.132]

D. G. Bhandari, S. J. MiUar, C. N. G. Scotter. Prediction of wheat protein and HMW-glutenin contents by near infrared (NIR) spectroscopy. Spec Publ R Soc Chem 261 313-316, 2000. [Pg.292]

B. W. Seabourn, S. R. Bean, G. L. Lookhart, O. K. Chung. Prediction of gliadin and soluble/insoluble HMW glutenin fractions in whole kernel wheat by near-infrared reflectance spectroscopy. Cereal Foods World, 43 518, 1998. [Pg.295]

Salmanowicz BP, Surma M, Adamski T, R barz M 2008. Effects of amounts of HMW glutenin subunits determined by capillary electrophoresis on technological properties in wheat doubled haploids. J Sci Food Agric 88 1716-1725. [Pg.112]


See other pages where HMW glutenin is mentioned: [Pg.294]    [Pg.303]    [Pg.304]    [Pg.306]    [Pg.307]    [Pg.481]    [Pg.482]    [Pg.486]    [Pg.397]    [Pg.397]    [Pg.399]    [Pg.372]    [Pg.72]    [Pg.76]    [Pg.76]    [Pg.116]    [Pg.133]    [Pg.133]    [Pg.157]    [Pg.157]    [Pg.157]    [Pg.357]   
See also in sourсe #XX -- [ Pg.681 , Pg.686 ]




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