title: Characterization of Cinnamoyl Esterases from Different Lactobacilli and Bifidobacteria.
abstract: A high variety of plants that are used for food production contain esterified hydroxycinnamic acids. As their free forms display several benefits, like an enhanced absorption in human intestinal tract, anti-oxidative and anti-carcinogenic effects, an improved protein solubility and reduced discoloration, the microbial ability to cleave the ester bond is highly desired. In order to examine potential fermentation strains for this purpose, six different lactic acid bacteria and one bifidobacterial strain were screened for their ability to degrade esterified hydroxycinnamic acids because these strains are commonly used for fermentation of plant-based foods. Moreover, their cinnamoyl esterase activity was examined by molecular biological analyses. The enzymes were heterologously expressed in Escherichia coli, purified and biochemically characterized. The purified esterases with a molecular mass around 27-29 kDa had their optimum predominantly between pH 7 and 8 at 20-30 °C. Bifidobacterium animalis subsp. lactis, Lactobacillus gasseri, Lactobacillus acidophilus, Lactobacillus plantarum and Lactobacillus fermentum displayed activities against a broad substrate range (methyl caffeate, methyl trans-p-coumarate, chlorogenic acid as well as partially ethyl ferulate). Concerning substrate affinity, reaction velocity, thermal and pH stability, Lactobacillus gasseri showed the overall best performance. The herein studied lactic acid- and bifidobacteria are promising for the production of fermented plant-based foods with an increased quality and nutritional value.
authors.affiliation: Fraunhofer Institute for Process Engineering and Packaging IVV, Giggenhauser Straße 35, Freising, Germany.
authors.forename: Caroline
authors.initials: C
authors.lastname: Fritsch
authors.affiliation: Technische Universität München, Technische Mikrobiologie Weihenstephan, Gregor-Mendel-Straße 4, Freising, Germany.
authors.forename: André
authors.initials: A
authors.lastname: Jänsch
authors.affiliation: Technische Universität München, Technische Mikrobiologie Weihenstephan, Gregor-Mendel-Straße 4, Freising, Germany. matthias.ehrmann@wzw.tum.de.
authors.forename: Matthias A
authors.initials: MA
authors.lastname: Ehrmann
authors.affiliation: Fraunhofer Institute for Process Engineering and Packaging IVV, Giggenhauser Straße 35, Freising, Germany.
authors.forename: Simone
authors.initials: S
authors.lastname: Toelstede
authors.affiliation: Technische Universität München, Technische Mikrobiologie Weihenstephan, Gregor-Mendel-Straße 4, Freising, Germany.
authors.forename: Rudi F
authors.initials: RF
authors.lastname: Vogel
mesh_terms: D001644:Bifidobacterium / Q000201:enzymology* / Q000235:genetics; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D003001:Cloning, Molecular; D003373:Coumaric Acids / Q000378:metabolism; D004795:Enzyme Stability; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D006863:Hydrogen-Ion Concentration; D007778:Lactobacillus / Q000201:enzymology* / Q000235:genetics; D008970:Molecular Weight; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D003373:Coumaric Acids; D011994:Recombinant Proteins; D002265:Carboxylic Ester Hydrolases; C070196:feruloyl esterase