ABSTRACT
Physical instability and loss of viability of probiotic bacteria are the most important problems in production of synbiotic Doogh. Some plant hydrocolloids have been recognised as effective components to prevent these problems. In this study the effect of Plantago psyllium mucilage (PPM) (0, 0.15%, 0.30%, 0.75% (w/w) on the physicochemical, microbial, and sensory properties of Doogh samples was evaluated by measuring phase separation, viscosity, flow behaviour, probiotic viability and sensory parameters. The results revealed that the stability of samples containing PPM were higher than samples without this hydrocolloid. By increasing the amounts of PPM, the viscosity of treated samples were increased compared to control sample. Herschel-Bulkley rheological model was an appropriate model for describing the flow behavior of Doogh formulated with PPM and the power-law rheological model was suitable model for describing the flow behavior of control samples. PPM had non-digestible food ingredients and improved the viability of Lactobacillus casei; therefore, this herbal mucilage may have prebiotic potential. Finally, the samples treated with 0.30% PPM on the 15th day were chosen as the best formulation for the production.
ABSTRACT
This study investigated the antibacterial properties of plasmin, the plasmin hydrolysis of bovine κ-casein and the fractions (named κC1, κC2, κC3, κC4, and κC5) liberated from it using RP-HPLC. The target bacteria were Escherichia coli, Staphylococcus aureus (pathogenic), Lactobacillus casei and Lactobacillus acidophilus (probiotic). Three peptides (kC1, kC3, and kC4) were found to have antibacterial activity, with κC3 peptide being the most active. The plasmin digest of bovine κ-casein proved to be stronger than any of its fractions in terms of antibacterial potential. Measurement of the minimum inhibitory concentration (MIC) showed that Gram-positive bacteria are generally more sensitive to antibacterial activity than Gram-negative bacteria. The MIC of nisin, as a bacteriocin peptide, was also measured. The three antibacterial peptides were identified using LC-Mass. The molecular mass of kC1, kC3, and kC4 corresponded to the f(17-21), f(22-24), and f(1-3) of bovine κ-casein, respectively. It was also found that the positive charge and hydrophobicity of a peptide are not key factors in antibacterial activity. On the whole, the present study demonstrated that the plasmin digest of κ-casein has a high antibacterial potential and can be considered as a natural antibacterial agent in the food chain.
