Utilize este identificador para referenciar este registo: http://hdl.handle.net/10400.14/6826
Título: Hydrolysis of α-lactalbumin by cardosin A immobilized on highly activated supports
Autor: Barros, Rui M.
Extremina, Clara I.
Gonçalves, Inês C.
Braga, Beatriz O.
Balcão, Victor M.
Malcata, F. Xavier
Palavras-chave: Enzyme
Structural stabilization
Dairy foods
Data: 2003
Editora: Elsevier
Citação: BARROS, Rui M... [et al.] - Hydrolysis of α-lactalbumin by cardosin A immobilized on highly activated supports. Enzyme and Microbial Technology. ISSN: 0141-0229. Vol. 33, n.º 7 (2003) p. 908-916
Resumo: In the present research effort, production of derivatives of cardosin A (a plant protease) encompassing full stabilization of its dimeric structure has been achieved, 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 providing evidence for the effectiveness of the attachment procedure. Furthermore, the cardosin A derivatives prepared under optimal conditions presented ca. half the specific activity of the enzyme in soluble form, and were successfully employed at laboratory-scale trials to perform (selective) hydrolysis of α-lactalbumin (α-La), one of the major proteins in bovine whey. Hydrolysates of α-La were assayed for by the OPA method, as well as by FPLC, SDS–PAGE and HPLC. Thermal inactivation of the immobilized cardosin A was also assessed at 40, 50 and 55 °C; at these temperatures, no thermal denaturation took place during incubation for 48 h. The highest degree of hydrolysis was attained by 5 h reaction, at 55 °C and pH 5.2. SDS–PAGE of α-La hydrolysates displayed bands corresponding to low molecular weight peptides. Our results suggest that cardosin A in immobilized form is a good candidate to bring about proteolysis in the dairy industry, namely in whey processing.
Peer review: yes
URI: http://hdl.handle.net/10400.14/6826
Versão do Editor: DOI: 10.1016/S0141-0229(03)00244-8
Aparece nas colecções:ESB - Artigos em revistas internacionais com Arbitragem / Papers in international journals with Peer-review

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