Molecular characterization of peptides released from beta-lactoglobulin and alpha-lactalbumin via cardosins A and B

• Type: Article in International Scientific Journal
• Date: 2006

Authors

Barros, RM (Author) Other; F. Xavier Malcata (Author) Other

Journal

Title: Journal of Dairy Science

Vol. 89 No. 7

Pages: 483-494

ISSN: 0022-0302

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 14 Citations

Scopus - 17 Citations

Other information

Authenticus ID: P-004-NFT

Abstract (EN): Crude mixtures of aspartic proteases from flowers of the plant Cynara cardunculus have been studied frequently, as have activities of such enzymes (in pure form) on caseins from bovine, ovine, and caprine sources. This research study addressed pure bovine whey protein as substrates; that is, a-lactalbumin (alpha-LA) and beta-lactoglobulin (alpha-LG), submitted to hydrolysis by 1 of 2 aspartic proteases (cardosins A and B), previously extracted and purified from C. cardunculus. Samples collected, following incubation at 55 degrees C and pH 5.2, were assayed by fast protein liquid chromatography, reversed phase-high performance liquid chromatography, and tricine-sodium dodecyl sulfate polyacrylamide gel electrophoresis; the major peptides released were then collected and sequenced by Edman degradation. Cardosin B and, to a lesser degree, cardosin A showed proteolytic activity toward alpha-LA, but the hydrolyzates produced were characterized by distinct peptide profiles. Cardosin B possesses a broad specificity, and produces several hydrophobic peptides (at least 5, with molecular mass in the range 2 to 8 kDa) in the early stages, which eventually become more hydrophilic (with molecular mass below 2 kDa) at later stages of hydrolysis. Cardosin A was found to cleave alpha-LA at the peptide bonds Phe28-Arg29, Gly54-Tyr55, Ala59-Ile60, Leu71-Phe72, and Leu105-Thr106, whereas cardosin B cleaved Ala19-Glu20, Phe28-Arg29, Glu30-Leu31, Tyr37-Gly38, Trp45-Val46, Phe50-His51, Ala59-Ile60, Ser66-Thr67, Leu71-Phe72, Phe72-Gln73, Gln73-Ile74, Ile78-Trp79, Leu115-Asp116, and Leu124-Ala125. Conversely, cardosins A and B are apparently not active on beta-LG.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 12