Food-fermenting lactobacilli convert glycosylated phytochemicals
to glycosyl hydrolases and thereby alter their biological activity.
This study aimed to investigate the microbial transformation of β-glucosides
of phytochemicals in comparison with utilization of cellobiose. Four
homofermentative and four heterofermentative lactobacilli were selected
to represent the metabolic diversity of Lactobacillaceae. The genomes of Lactobacillus crispatus, Companilactobacillus paralimentarius, Lacticaseibacillus paracasei, and Lactiplantibacillus plantarum encoded for 8 to 22
enzymes, predominantly phospho-β-glucosidases, with predicted
activity on β-glucosides. Levilactobacillus hammesii and Furfurilactobacillus milii encoded
for 3 β-glucosidases, Furfurilactobacillus rossiae for one, and Fructilactobacillus sanfranciscensis for none. The hydrolysis of amygdalin, esculin, salicin, glucosides
of quercetin and genistein, and ginsenosides demonstrated that several
strains hydrolyzed β-glucosides of phytochemicals but not cellobiose.
Taken together, several of the carbohydrate-active enzymes of food-fermenting
lactobacilli are specific for glycosides of phytochemicals.