Adhesive Interactions Between Lactic Acid Bacteria and β-Lactoglobulin: Specificity and Impact on Bacterial Location in Whey Protein Isolate

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Gomand, Faustine | Borges, Frédéric | Guerin, Justine | El-Kirat-Chatel, Sofiane | Francius, Gregory | Dumas, Dominique | Burgain, Jennifer | Gaiani, Claire

Edité par CCSD ; Frontiers Media -

International audience. 15 In the last decade, there has been an increasing interest in the potential health effects associated with 16 the consumption of Lactic Acid Bacteria (LAB) in foods. Some of these bacteria such as Lactobacillus 17 rhamnosus GG (LGG) are known to adhere to milk components, which may impact their distribution 18 and protection within dairy matrices and therefore is likely to modulate the efficiency of their delivery. 19 However, the adhesive behavior of most LAB, as well as its effect on food structuration and on the 20 final bacterial distribution within the food matrix remain very poorly studied. Using a recently 21 developed high-throughput approach, we have screened a collection of 73 LAB strains for their 22 adhesive behavior towards the major whey protein β-lactoglobulin. Adhesion was then studied by 23 genomics in relation to common bacterial surface characteristics such as pili and adhesion-related 24 domain containing proteins. Representative adhesive and non-adhesive strains have been studied in 25 further depth through biophysical measurement using Atomic Force Microscopy (AFM) and a relation 26 with bacterial distribution in Whey Protein Isolate (WPI) solution has been established. AFM 27 measurements have revealed that bacterial adhesion to β-lactoglobulin is highly specific and cannot be 28 predicted accurately using only genomic information. Non-adhesive strains were found to remain 29 homogeneously distributed in solution whereas adhesive strains gathered in flocs. These findings show 30 that several LAB strains are able to adhere to β-lactoglobulin, whereas this had only been previously 31 observed on LGG. We also show that these adhesive interactions present similar characteristics and 32 are likely to impact bacterial location and distribution in dairy matrices containing β-lactoglobulin. 33 This may help with designing more efficient dairy food matrices for optimized LAB delivery. 34

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