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

• Type: Article in International Scientific Journal
• Date: 2001

Authors

Lamas, EM (Author) Other; Barros, RM (Author) Other; Balcao, VM (Author) Other; F. Xavier Malcata (Author) Other

Journal

Title: Enzyme and Microbial Technology

Vol. 28

Pages: 642-652

ISSN: 0141-0229

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 50 Citations

Scopus - 65 Citations

Other information

Authenticus ID: P-000-VHR

DOI: 10.1016/s0141-0229(01)00308-8

Abstract (EN): 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 stigma: and stylets of said flowers, and an 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 beta -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 alpha -lactalbumin, one of the major proteins in bovine whey.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 11