Utilize este identificador para referenciar este registo: http://hdl.handle.net/10400.14/6836
Título: Hydrolysis of whey proteins by proteases extracted from Cynara cardunculus and immobilized onto highly activated supports
Autor: Lamasa, Estela M.
Barrosa, Rui M.
Balcão, Victor M.
Malcata, F. Xavier
Palavras-chave: Enzyme
Cardosin
Agarose
Structural stabilization
Dairy foods
Hydrolase
Attachment
Data: 2001
Editora: Elsevier
Citação: LAMASA, Estela M.... [et al.] - Hydrolysis of whey proteins by proteases extracted from Cynara cardunculus and immobilized onto highly activated supports.Enzyme and Microbial Technology. ISSN 0141-0229. Vol. 28, n.º 7-8 (2001), p. 642–652
Resumo: 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.
Peer review: yes
URI: http://hdl.handle.net/10400.14/6836
Versão do Editor: doi:10.1016/S0141-0229(01)00308-8
Aparece nas colecções:ESB - Artigos em revistas internacionais com Arbitragem / Papers in international journals with Peer-review

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