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Comparative Digestibility of Legume Storage Proteins
Journal of Agricultural and Food Chemistry (1988)
  • S. Suzanne Nielsen, Purdue University
  • Marvin Paul Scott, Purdue University
  • Sudhir S. Deshpande, University of Wisconsin-Madison
  • Mark A. Hermodson, Purdue University
Native and heated legume storage proteins were digested with various proteinases. Gel electrophoresis
patterns indicated that phaseolin (dry bean) was most resistant to digestion, vicilin (pea) was most
susceptible, and glycinin and P-conglycinin (soybean) were intermediate in susceptibility to various
proteinases. The native proteins were cleaved by trypsin and chymotrypsin in only limited areas of
the molecule, but they were all readily degraded upon heating. N-Terminal sequence analysis of the
major breakdown products from phaseolin digestion and hydrophilicity and surface probability determinations
indicated that trypsin, chymotrypsin, and papain cleave native phaseolin near the center
of the protein molecule at a hydrophilic region predicted to be on the surface. This region in phaseolin
is highly homologous in sequence with hydrophilic regions in vicilin and P-conglycinin.
Publication Date
September, 1988
Publisher Statement
This article is from Journal of Agricultural and Food Chemistry 36 (1988): 896, doi: 10.1021/jf00083a004
Citation Information
S. Suzanne Nielsen, Marvin Paul Scott, Sudhir S. Deshpande and Mark A. Hermodson. "Comparative Digestibility of Legume Storage Proteins" Journal of Agricultural and Food Chemistry Vol. 36 Iss. 5 (1988) p. 896 - 902
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