Batch foam recovery of sporamin from sweet potato

Appl Biochem Biotechnol. 1998 Spring:70-72:547-58. doi: 10.1007/BF02920167.

Abstract

The major sweet potato root protein, sporamin (which comprises about 80-90% of the total protein mass in the sweet potato) easily foams in a bubble/foam-fractionation column using air as the carrier gas. Control of that foam fractionation process is readily achieved by adjusting two variables: bulk solution pH and gas superficial velocity. Varying these parameters has an important role in the recovery of sporamin in the foam. Changes in the pH of the bulk solution can control the partitioning of sporamin in the foam phase from that in the bulk phase. A change in pH will also affect the amount of foam generated. The pH varied between 2.0 and 10.0 and the air superficial velocities (V0) ranged between 1.5 and 4.3 cm/s. It was observed in these ranges that, as the pH increased, the total foamate volume decreased, but the foamate protein (mainly sporamin) concentration increased. On the other hand, the total foamate volume increased significantly as the air superficial velocity increased, but the foamate concentration decreased slightly. The minimum residual protein concentration occurred at pH 3.0 and V0 = 1.5 cm/s. On the other hand, the maximum protein mass recovery occurred at pH 3.0 and at V0 = 4.3 cm/s.

MeSH terms

  • Chemical Fractionation
  • Hydrogen-Ion Concentration
  • Molecular Weight
  • Plant Proteins / isolation & purification*
  • Plant Roots / chemistry
  • Solanaceae / chemistry*
  • beta-Amylase / isolation & purification

Substances

  • Plant Proteins
  • sporamin protein, Ipomoea batatas
  • beta-Amylase