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Val bean (Lablab purpureus L.) proteins: composition and biochemical properties by Mahesh Venkatachalam; Shridhar K Sathe is a Agricultural and Biological Sciences article available to read on EtoBox.

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## Abstract __Val__ bean (__Lablab purpureus__ L.) proteins were fractionated using the Osborne protein fractionation scheme and biochemically characterized. The seed flour contained 302 g kg^−1^ protein (micro‐Kjeldahl N × 6.25) on a dry weight basis. Albumin, globulin, prolamin, and glutelin accounted for 22.8%, 45.1%, 1.8% and 30.3%, respectively, of the total soluble seed proteins. Among the solvents tested, 0.1 mol L^−1^ aqueous NaOH was the most effective protein solubilizer. Isoelectric focusing indicated the seed proteins to be predominantly acidic (p__I__ range was ∼4–7). __Val__ globulin is a glycoprotein composed of at least three polypeptides in the molecular mass range 51–64 kDa. Albumin fraction had the highest trypsin inhibitory activity, while the globulin fraction registered the highest hemagglutinating activity. Sulfur amino acids were the first limiting amino acids in the total seed proteins. The proportion of essential to total [__E__/__T__(%)] amino acids for the bean flour was 36.97%. Among the protein fractions, glutelin fraction had the highest __E__/__T__ (42.86%) followed by albumin (41.57%), globulin (39.87%), and prolamin (39.15%). Native globulin, altho

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Author

Mahesh Venkatachalam; Shridhar K Sathe

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0022-5142)

Published

2007

Language

EN

Field

Agricultural and Biological Sciences (Life Sciences)