Significance of bacterial surface molecules interactions with milk proteins to enhance microencapsulation of Lactobacillus rhamnosus GG

Impacts of pH-mediated EPS structure on probiotic bacterial pili–whey proteins interactions

“…This observation confirms the fact that pili establish interactions with proteins and more particularly whey proteins. These results support the conclusions drawn in our previous study on the role played by pili surface structures in the specific interactions between LGG and whey proteins [5]. …”

“…The spring constant of the probes is of 0.01 nN/nm. The tips for force measurements were coated with milk proteins by immersion for 15 h in the aforementioned solution, and then washed with milli-Q-grade water [5]. The protein-coated probes were rinsed into milli-Q water prior to use.…”

“…In a previous study [4], the interactions between LGG and dairy proteins were explored by atomic force spectroscopy. The results evidenced that pili at LGG cell surface were engaged in specific interactions with the whey protein fraction, but not with casein micelles [4,5]. Pili are thread-like structures with length up to 1 m. The SpaC pilin located along the pilus shaft and at the tip has the ability to bind human mucus [6].…”

Preparation and properties of milk proteins-based encapsulated probiotics: a review

“…The efficiency of encapsulation of the Lactobacillus rhamnosus GG (LGG) wild type and mutants lacking exopolysaccharide, with modified surface charge and lacking pili, was compared. The mutant lacking the SpaCBA pili was the least to interact with casein and whey protein matrices (Burgain et al 2014). Also, the pilus appeared to be crucial for location of the LGG inside the microcapsule (Burgain et al 2014).…”

“…The mutant lacking the SpaCBA pili was the least to interact with casein and whey protein matrices (Burgain et al 2014). Also, the pilus appeared to be crucial for location of the LGG inside the microcapsule (Burgain et al 2014). …”