Hydrolysis of whey proteins by proteases extracted from Cynara cardunculus and immobilized onto highly activated supports

Estela M. Lamas, Rui M. Barros, Victor M. Balcão, F. Xavier Malcata*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

67 Citations (Scopus)

Abstract

Blends of cardosins A and B, enzymes present in aqueous extracts of the flowers of the thistle (Cynara cardunculus L.), have for long been used as rennets by the cheesemaking industry in the Iberian Peninsula. These dimeric proteases are present in the stigmæ and stylets of said flowers, and are thought to play a role in sexual reproduction of the plant. In the present research effort, production of cardosin derivatives (starting from a crude extract), encompassing full stabilization of their dimeric structure, has been attempted via covalent, multi-subunit immobilization onto highly activated agarose-glutaraldehyde supports. Boiling such enzyme derivatives in the presence of sodium dodecyl sulfate and β-mercaptoethanol did not lead to leaching of enzyme, thus proving the effectiveness of the attachment procedure. Furthermore, derivatives prepared under optimal conditions presented ca. half the specific activity of the enzyme in soluble form, and were successfully employed at lab-scale trials to perform (selective) hydrolysis of α-lactalbumin, one of the major proteins in bovine whey.
Original languageEnglish
Pages (from-to)642-652
Number of pages11
JournalEnzyme and Microbial Technology
Volume28
Issue number7-8
DOIs
Publication statusPublished - 7 May 2001

Keywords

  • Agarose
  • Attachment
  • Cardosin
  • Dairy foods
  • Enzyme
  • Hydrolase
  • Structural stabilization

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