(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Terrabacteria group: NE > Firmicutes: NE > Bacilli: NE > Bacillales: NE > Bacillaceae: NE > Bacillus: NE > Bacillus altitudinis complex: NE > Bacillus altitudinis: NE
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MNLDEQIKMAESLRQPAEDSLAGQSELKPVHPPEVNKMEYDIPTGAGETK VWVFKPVKTLKQPLPVFVNLHGGGFILGSAEMDNHWCPVIADRAECIVVN VEYQLAPEHPFPAALHECYDVMKWLYEHPEELQIDPNRLAIGGHSAGGNL ATAVCLLDIQKGNKLPIVYQVLDYPPLDLATDPAQKPVFEEAIPVEMARL FNAFYLQGQDPHNPLVSPVFAEREVLAQMPPALVITAEKDSLAEEAEHYA DKLKEAGVDVTYKQFKGVPHAFTHAGDLEIAEEAWHLMSDQLKKAFE
A novel feruloyl esterase (BpFae12) with rosmarinic acid (RA) hydrolysis activity was isolated from Bacillus pumilus W3 and expressed in Escherichia coli BL21 (DE3). With RA as a substrate, the optimal pH and temperature of BpFae12 were pH 8.0 and 50 degreesC, respectively. The specific enzyme activity was 12.8 U.mg(-1). BpFae12 showed the highest activity and substrate affinity toward RA (V(max) of 13.13 U.mg(-1), K(m) of 0.41 mM). Moreover, it also presented strong hydrolysis performance against chlorogenic acid (190.17 U.mg(-1)). RA was effectively Hydrolyzed into more bioactive caffeic acid and 3,4-dihydroxyphenyllactic acid by BpFae12, which have potential applications in the food industry.
