Purification and biochemical characterization of 11S globulin from chan (Hyptis suaveolens L. Poit) seeds

Food Chem. 2016 Feb 1:192:203-11. doi: 10.1016/j.foodchem.2015.06.099. Epub 2015 Jun 30.

Abstract

Chan (Hyptis suaveolens) is a Mesoamerican crop highly appreciated since the pre-Hispanic cultures. Its proteins are a good source of essential amino acids; however, there are no reports on the properties of its individual proteins. In this study, the 11S globulin (Hs11S) was purified and biochemically characterized. The molecular weight of native Hs11S was about 150-300 kDa with isoelectric points of 5.0-5.3, composed by four monomers of 53.5, 52, 51.1 and 49.5 kDa, each formed by one acidic subunit and one basic subunit linked by a disulfide bond. Dynamic light scattering, size exclusion chromatography and native PAGE show that Hs11S is assembled in different oligomeric forms. LC-MS/MS analysis confirmed its identity. Hs11S presents antigenic determinants in common with lupin 11S globulin. Carbohydrate moieties or phosphate groups linked to Hs11S were not detected. This information is very useful in order to exploit and utilize rationally chan 11S globulin in food systems.

Keywords: 11S globulin; Biochemical characterization; Dynamic light scattering; Hyptis suaveolens; Mass spectrometry; Seed storage proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Electrophoresis, Polyacrylamide Gel
  • Globulins / isolation & purification*
  • Hyptis / chemistry*
  • Isoelectric Point
  • Molecular Weight
  • Seed Storage Proteins / isolation & purification*
  • Seeds / chemistry*
  • Tandem Mass Spectrometry

Substances

  • Globulins
  • Seed Storage Proteins