Reconstituted skim milk was gelled at 25-40°C with the plant-origin coagulants from Cynara cardunculus L. or Cynara humilis L. or with fermentation-produced chymosin. Gel formation and ageing were monitored by low amplitude oscillatory rheology and confocal scanning laser microscopy. Arrhenius plots for the rate of milk gelation were also determined. Plant coagulants had shorter gelation time (tg) at 25°C, 35°C...
The rheological properties of milk gels made using coagulants obtained from the plants Cynara cardunculus L. and Cynara humilis L. were compared with those of fermentation-produced chymosin, using dynamic low amplitude oscillation as well as large strain (yield) testing. Gelation experiments were performed at 32°C using skim milk powder that had been reconstituted for 2 or 16 h at 32°C. The storage modulus (G')...
The action of cardosin on bovine αs- and β-casein at 30 °C in 50 mM citrate buffer (pH 6.2) was studied. Peptides were isolated by reversed-phase HPLC on C18 columns and identified from their amino acid composition and N-terminal amino acid sequence. The relative susceptibility of peptide bonds cleaved was Phe23-Phe24 > Trp164-Tyr165 > Tyr166-Val167 > Tyr165-Tyr166 > Phe153-Tyr154 > Phe145-Tyr146 ≈ Leu149-Phe15...
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 glyco...
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