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https://hdl.handle.net/10316/12876
Title: | Specificity and kinetics of the milk-clotting enzyme from cardoon (Cynara cardunculus L.) toward bovine .kappa.-casein | Authors: | Macedo, I. Queiroz Faro, Carlos J. Pires, Euclides M. |
Issue Date: | Oct-1993 | Publisher: | American Chemical Society | Citation: | Journal of Agricultural and Food Chemistry. 41:10 (1993) 1537-1540 | Abstract: | The action of Cynara cardunculus L. protease on whole bovine K-casein, over a 3-h period at pH 6.4, was investigated. RpHPLC of the 3% trichloroacetic acid (TCA)-solublefraction of the K-casein digestion mixture showed three peptide peaks, which were identified by amino acid analysis and N-terminal analysis as the 106-169 fragment [caseinomacropeptide (CMP)]. Upon selective precipitation with 12% TCA, one glycosylated and two nonglycosylated forms of CMP were distinguished. Analysis of the whole digestion mixture showed no additional peptides. The kinetics of hydrolysis of the PhelO5- Met106 bond was studied by spectrofluorometry, using fluorescein isothiocyanate-labeled K-casein (FTC- K-casein). The values obtained for kat, k, and k were 1.04 s-l, 0.16 pM, and 6.5 pM-l s-l, respectively. The proteolytic coefficient is of the same order of magnitude as those obtained for other milk-clotting enzymes, but the k, is significantly lower, which reflects the higher affinity of Cynara protease to K-casein | URI: | https://hdl.handle.net/10316/12876 | ISSN: | 0021-8561 | DOI: | 10.1021/jf00034a001 | Rights: | openAccess |
Appears in Collections: | FCTUC Ciências da Vida - Artigos em Revistas Internacionais |
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Specificity and kinetics of the milk-clotting enzyme.pdf | 489.63 kB | Adobe PDF | View/Open |
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