Peptides with biological and technofunctional properties produced by bromelain hydrolysis of proteins from different sources: A review

Int J Biol Macromol. 2023 Dec 31;253(Pt 5):127244. doi: 10.1016/j.ijbiomac.2023.127244. Epub 2023 Oct 6.

Abstract

Bromelains are cysteine peptidases with endopeptidase action (a subfamily of papains), obtained from different parts of vegetable belonging to the Bromeliaceae family. They have some intrinsic medical activity, but this review is focused on their application (individually or mixed with other proteases) to produce bioactive peptides. When compared to other proteases, perhaps due to the fact that they are commercialized as an extract containing several proteases, the hydrolysates produced by this enzyme tends to have higher bioactivities than other common proteases. The peptides and the intensity of their final properties depend on the substrate protein and reaction conditions, being the degree of hydrolysis a determining parameter (but not always positive or negative). The produced peptides may have diverse activities such as antioxidant, antitumoral, antihypertensive or antimicrobial ones, among others or they may be utilized to improve the organoleptic properties of foods and feeds. Evolution of the use of this enzyme in this application is proposed to be based on a more intense direct application of Bromeliaceae extract, without the cost associated to enzyme purification, and the use of immobilized biocatalysts of the enzyme by simplifying the enzyme recovery and reuse, and also making the sequential hydrolysis using diverse proteases possible.

Keywords: Combiproteases; Hydrolysis degree; Protein hydrolysis.

Publication types

  • Review

MeSH terms

  • Bromelains* / chemistry
  • Endopeptidases / chemistry
  • Hydrolysis
  • Peptide Hydrolases / metabolism
  • Peptides* / chemistry
  • Protein Hydrolysates / chemistry

Substances

  • Bromelains
  • Peptides
  • Peptide Hydrolases
  • Endopeptidases
  • Protein Hydrolysates