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B. Khatkar, A. Bell, J. Schofield (1995)
The Dynamic Rheological Properties of Glutens and Gluten Sub-Fractions from Wheats of Good and Poor Bread Making QualityJournal of Cereal Science, 22
N. Chaudhary, P. Dangi, B. Khatkar (2017)
Fractionation of unreduced gluten proteins on SEC and their relationship with cookie quality characteristicsJournal of Food Science and Technology, 54
BS Khatkar (2006)
Effect of high Mr glutenin subunits on dynamic rheological properties and bread making qualities of wheat gluteninJ Food Sci Technol, 43
Y. Nicolas, J. Martinant, S. Denery-Papini, Y. Popineau (1998)
Analysis of wheat storage proteins by exhaustive sequential extraction followed by RP‐HPLC and nitrogen determinationJournal of the Science of Food and Agriculture, 77
M. Sissons, F. Békés, J. Skerritt (1998)
Isolation and Functionality Testing of Low Molecular Weight Glutenin SubunitsCereal Chemistry, 75
N. Chaudhary, P. Dangi, B. Khatkar (2016)
Evaluation of molecular weight distribution of unreduced wheat gluten proteins associated with noodle qualityJournal of Food Science and Technology, 53
O. Larroque, M. Gianibelli, I. Batey, F. Macritchie (1997)
Electrophoretic characterisation of fractions collected from gluten protein extracts subjected to size‐exclusion high‐performance liquid chromatographyELECTROPHORESIS, 18
P Dangi, BS Khatkar (2017)
Physicochemical and gluten quality characteristics of commercial wheat varietiesInt J Innov Res Sci Eng Technol, 6
P Dangi, BS Khatkar (2017)
Effect of glutenin addition on dough mixing characteristics of wheat varietiesInt J Innov Res Sci Eng Technol, 6
B. Khatkar, J. Schofield (1997)
Molecular and physico-chemical basis of breadmaking : Properties of wheat gluten proteins : A critical appraisalJournal of Food Science and Technology-mysore, 34
AC Beckwith, HC Neilsen, JS Wall, FR Huebner (1966)
Isolation and characterization of high-molecular weight protein from wheat gliadinCereal Chem, 43
N. Chaudhary, P. Dangi, B. Khatkar (2016)
Relationship of molecular weight distribution profile of unreduced gluten protein extracts with quality characteristics of bread.Food chemistry, 210
BS Khatkar, JD Schofield (1997)
Molecular and physicochemical basis of bread making properties of wheat gluten proteinsJ Food Sci Technol, 34
R. D'Ovidio, S. Masci (2004)
The low-molecular-weight glutenin subunits of wheat glutenJournal of Cereal Science, 39
C. Larré, Y. Nicolas, C. Desserme, P. Courcoux, Y. Popineau (1997)
Preparative separation of high and low molecular weight subunits of glutenin from wheatJournal of Cereal Science, 25
N. Chaudhary, P. Dangi, B. Khatkar (2016)
Assessment of molecular weight distribution of wheat gluten proteins for chapatti quality.Food chemistry, 199
V. Dhaka, B. Khatkar (2015)
Effects of Gliadin/Glutenin and HMW‐GS/LMW‐GS Ratio on Dough Rheological Properties and Bread‐Making Potential of Wheat VarietiesJournal of Food Quality, 38
E. Lew, D. Kuzmicky, D. Kasarda (1992)
Characterization of low molecular weight glutenin subunits by reversed-phase high-performance liquid chromatography, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and N-terminal amino acid sequencingCereal Chemistry, 69
Wim Veraverbeke, J. Delcour (2002)
Wheat Protein Composition and Properties of Wheat Glutenin in Relation to Breadmaking FunctionalityCritical Reviews in Food Science and Nutrition, 42
Crude glutenin of four commercial wheat varieties viz. C 306, HI 977, HW 2004 and PBW 550 of diverse origin and breadmaking quality were fractionated by size-exclusion chromatography into three fractions of decreasing molecular weights. The relative quantity of peak II, containing LMW-GS specifically, varied considerably among the varieties as reflected from their discrete SEC profiles. The area % of peak II, containing protein of interest, was maximal for C 306 (22.08%) followed by PBW 550 (15.86%). The least proportion of LMW-GS were recovered from variety HW 2004 (9.68%). As the concentration of the sample extract injected to the column increased, the resolution of the peak declined in association with the slight shifting of retention time to the higher values. The best results were obtained for variety C 306 at 100 mg protein concentration with 3 M urea buffer. Consequently, the optimized conditions for purification of LMW-GS in appreciable amounts using SEC were established.
Journal of Food Science and Technology – Springer Journals
Published: Jan 12, 2018
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