TY - JOUR
T1 - Co-immobilized β-galactosidase and Saccharomyces cerevisiae cells for the simultaneous synthesis and purification of galacto-oligosaccharides
AU - Aburto, Carla
AU - Guerrero, Cecilia
AU - Vera, Carlos
AU - Wilson, Lorena
AU - Illanes, Andrés
N1 - Funding Information:
This work was financed by Chilean Fondecyt Grant 1130059 , the scholarships 21120651 from Conicyt, Chile and the Direction of Research, Innovation and Graduate Studies of the Universidad Técnica Federico Santa María . We acknowledge the generous donations of A. oryzae β-galactosidase by Enzyme Development Corporation (New York, USA).
Publisher Copyright:
© 2018 Elsevier Inc.
PY - 2018/11
Y1 - 2018/11
N2 - Simultaneous synthesis and purification (SSP) of galacto-oligosaccharides (GOS) from lactose was conducted using a combi-biocatalyst formed by crosslinked enzyme aggregates of Aspergillus oryzae β-galactosidase and Saccharomyces cerevisiae cells co-immobilized by entrapment in calcium alginate gel particles. Product yield obtained with the combi-biocatalyst was similar than obtained with the soluble enzyme (23.3%), having a final purity of 25.7%. During the simultaneous process, ethyl-β-galactoside was produced from the ethanol generated as a metabolic product of yeast cells, but ethyl-β-galactoside was considerably decreased at high aeration (4 vvm). The combi-biocatalyst can be recovered and reused but its performance is limited by the reduction of the metabolic capacity of the cells. In this way, a process was developed for the SSP of GOS from lactose, obtaining a comparable product yield and higher specific productivity than in a conventional synthesis.
AB - Simultaneous synthesis and purification (SSP) of galacto-oligosaccharides (GOS) from lactose was conducted using a combi-biocatalyst formed by crosslinked enzyme aggregates of Aspergillus oryzae β-galactosidase and Saccharomyces cerevisiae cells co-immobilized by entrapment in calcium alginate gel particles. Product yield obtained with the combi-biocatalyst was similar than obtained with the soluble enzyme (23.3%), having a final purity of 25.7%. During the simultaneous process, ethyl-β-galactoside was produced from the ethanol generated as a metabolic product of yeast cells, but ethyl-β-galactoside was considerably decreased at high aeration (4 vvm). The combi-biocatalyst can be recovered and reused but its performance is limited by the reduction of the metabolic capacity of the cells. In this way, a process was developed for the SSP of GOS from lactose, obtaining a comparable product yield and higher specific productivity than in a conventional synthesis.
KW - Ethyl-β-galactoside
KW - GOS purification
KW - Galacto-oligosaccharides
KW - β-galactosidase
UR - http://www.scopus.com/inward/record.url?scp=85051266812&partnerID=8YFLogxK
U2 - 10.1016/j.enzmictec.2018.08.003
DO - 10.1016/j.enzmictec.2018.08.003
M3 - Article
C2 - 30143193
AN - SCOPUS:85051266812
VL - 118
SP - 102
EP - 108
JO - Enzyme and Microbial Technology
JF - Enzyme and Microbial Technology
SN - 0141-0229
ER -