The effect of heat treatment on the soluble protein content of oats |
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| Affiliation: | 1. Lund Centre for Field-Flow Fractionation, Department of Food Technology, Engineering and Nutrition, Lund University, Lund, Sweden;2. SOLVE Research and Consultancy AB, Lund, Sweden;3. Department of Applied Nutrition and Food Chemistry, Lund University, Lund, Sweden;1. Wageningen UR Plant Breeding, Wageningen University and Research Centre, P. O. Box 386, NL-6700 AJ Wageningen, The Netherlands;2. Bioscience, Wageningen University and Research Centre, P.O. Box 16, NL-6700 AA Wageningen, The Netherlands;3. Allergy Consortium Wageningen, P.O. Box 16, NL-6700 AA Wageningen, The Netherlands;4. Wageningen UR Food Chemistry, Wageningen University and Research Centre, P. O. Box 8129, NL-6700 EV Wageningen, The Netherlands;1. VTT Technical Research Centre of Finland, Tietotie 2 02044 VTT, Finland;2. Kagawa University, Department of Applied Biological Science, 2393 Ikenobe, Miki-cho, Kita-gun, Kagawa 761-0795, Japan;1. College of Food Science and Technology, Nanjing Agricultural University, Nanjing, 210095, China;2. College of Food Science and Engineering, Nanjing University of Finance and Economics, Nanjing, 210023, China |
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| Abstract: | The effect of heat treatment on the soluble protein content in oat groats (Kerstin commercial variety) was evaluated using asymmetric flow field-flow fractionation (AF4) in combination with online multiangle light scattering (MALS) and UV detection. The AF4 method was used to separate the monomeric proteins from globulin hexamer and aggregate proteins and β-glucan polysaccharides in the soluble oat protein fraction. The total amount of soluble protein (with respect to total protein) was reduced to 35.7 ± 4.5 wt. % in heat treated oats from 74.6 ± 5.3 wt. % in non-heat treated oats. The ratio of monomeric to globulin hexamer and aggregate proteins was reduced from 1.82 to 1.48 as a result of heat treatment. Sodium-dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis revealed the selective elimination of protein bands associated with the albumin and prolamin protein fractions as a result of heat treatment. These results were supported through amino acid analysis by cation exchange chromatography coupled with UV detection which revealed a reduction in amino acid residues associated with prolamin. The globulin proteins were found to be less sensitive to heat treatment. |
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| Keywords: | Light scattering Field-flow fractionation Heat treatment Protein aggregates Oat proteins Beta glucans AF4" },{" #name" :" keyword" ," $" :{" id" :" kwrd0045" }," $$" :[{" #name" :" text" ," _" :" Asymmetric flow field-flow fractionation HPLC" },{" #name" :" keyword" ," $" :{" id" :" kwrd0055" }," $$" :[{" #name" :" text" ," _" :" High pressure liquid chromatography K" },{" #name" :" keyword" ," $" :{" id" :" kwrd0065" }," $$" :[{" #name" :" text" ," _" :" Kerstin non-heat treated oats KHT" },{" #name" :" keyword" ," $" :{" id" :" kwrd0075" }," $$" :[{" #name" :" text" ," _" :" Kerstin heat treated oats M" },{" #name" :" keyword" ," $" :{" id" :" kwrd0085" }," $$" :[{" #name" :" text" ," _" :" Molar mass mM" },{" #name" :" keyword" ," $" :{" id" :" kwrd0095" }," $$" :[{" #name" :" text" ," _" :" Millimolar MALS" },{" #name" :" keyword" ," $" :{" id" :" kwrd0105" }," $$" :[{" #name" :" text" ," _" :" Multi-angle light scattering SDS-PAGE" },{" #name" :" keyword" ," $" :{" id" :" kwrd0115" }," $$" :[{" #name" :" text" ," _" :" Sodium-dodecyl-sulfate polyacrylamide gel electrophoresis SEC" },{" #name" :" keyword" ," $" :{" id" :" kwrd0125" }," $$" :[{" #name" :" text" ," _" :" Size exclusion chromatography |
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