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Electrophoretic analysis reveals distinct seed protein fractions in ten bunch peanut varieties, highlighting molecular profiles for varietal identification.
Aim: To isolate these fractions, a progressive centrifugation technique was employed, utilizing water, sodium chloride, phosphate buffer, and alcohol. Place and Duration of Study: A study conducted in department of biochemistry Junagadh Agricultural University, Junagadh for analysis seeds of the bunch-type groundnut were supplied by the Main Oilseeds Research Station in Junagadh during 2020-2022. The Methodology Used: Using SDS-PAGE separation method, four key protein fractions: albumin, prolamin, globulin, and glutelin were analyzed. Results: The results revealed the highest albumin and globulin contents ranging from 15.05-20.81% and 69.91-77.99%, respectively. The globulin fraction was found to be significantly higher in proportion compared to the other three fractions. Glutelin and prolamin were found to be very low percentage-wise in bunch varieties but it was found to be in the range of 1.49-3.42 % in glutelin as well as prolamins were found to be in the range of 1.5-3.95%. The SDS-PAGE analysis of the ten-bunch type varieties revealed significant variations in protein profiles, as evidenced by the total number of bands and their respective molecular weight-retention factor (MW-Rf) values. The albumin and globulin fractions exhibited the highest MW-Rf values collectively, whereas glutelin and prolamin demonstrated minimal banding patterns. Conclusion: This study concludes that the observed qualitative and quantitative differences in seed protein profiles are invaluable for varietal identification.
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Gore et al. (2024) studied this question.
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