TY - JOUR
T1 - Β-Galactosidase from Exiguobacterium acetylicum
T2 - Cloning, expression, purification and characterization
AU - Aburto, Carla
AU - Castillo, Carlos
AU - Cornejo, Fabián
AU - Arenas-Salinas, Mauricio
AU - Vásquez, Claudio
AU - Guerrero, Cecilia
AU - Arenas, Felipe
AU - Illanes, Andrés
AU - Vera, Carlos
N1 - Publisher Copyright:
© 2019 Elsevier Ltd
PY - 2019/4
Y1 - 2019/4
N2 - The main goal of this work was to evaluate the performance of β-galactosidase from Exiguobacterium acetylicum MF03 in both hydrolysis and transgalactosylation reactions from different substrates. The enzyme gene was expressed in Escherichia coli BL21 (DE3), sequenced, and subjected to bioinformatic and kinetic assessment. Results showed that the enzyme was able to hydrolyze lactulose and o-nitrophenyl-β-D-galactopyranoside, but unable to hydrolyze lactose, o-nitrophenyl-β-D-glucopyranoside, butyl- and pentyl-β-D-galactosides. This unique and novel substrate specificity converts the E. acetylicum MF03 β-galactosidase into an ideal catalyst for the formulation of an enzymatic kit for lactulose quantification in thermally processed milk. This is because costly steps to eliminate glucose (resulting from hydrolysis of lactose when a customary β-galactosidase is used) can be avoided.
AB - The main goal of this work was to evaluate the performance of β-galactosidase from Exiguobacterium acetylicum MF03 in both hydrolysis and transgalactosylation reactions from different substrates. The enzyme gene was expressed in Escherichia coli BL21 (DE3), sequenced, and subjected to bioinformatic and kinetic assessment. Results showed that the enzyme was able to hydrolyze lactulose and o-nitrophenyl-β-D-galactopyranoside, but unable to hydrolyze lactose, o-nitrophenyl-β-D-glucopyranoside, butyl- and pentyl-β-D-galactosides. This unique and novel substrate specificity converts the E. acetylicum MF03 β-galactosidase into an ideal catalyst for the formulation of an enzymatic kit for lactulose quantification in thermally processed milk. This is because costly steps to eliminate glucose (resulting from hydrolysis of lactose when a customary β-galactosidase is used) can be avoided.
KW - Exiguobacterium acetylicum
KW - Lactose
KW - Lactulose
KW - β-Galactosidase
UR - http://www.scopus.com/inward/record.url?scp=85059766156&partnerID=8YFLogxK
U2 - 10.1016/j.biortech.2019.01.005
DO - 10.1016/j.biortech.2019.01.005
M3 - Article
C2 - 30639092
AN - SCOPUS:85059766156
SN - 0960-8524
VL - 277
SP - 211
EP - 215
JO - Bioresource Technology
JF - Bioresource Technology
ER -
