Premium
Hydrolysis of particulate tributyrin in a fluidized lipase reactor
Author(s) -
Lieberman R. B.,
Ollis D. F.
Publication year - 1975
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260171002
Subject(s) - michaelis–menten kinetics , tributyrin , substrate (aquarium) , adsorption , chemistry , lipase , chromatography , hydrolysis , fluidized bed , immobilized enzyme , reaction rate constant , chemical engineering , emulsion , mass transfer , kinetics , organic chemistry , enzyme assay , enzyme , quantum mechanics , oceanography , physics , engineering , geology
Abstract Pancreatic lipase has been immobilized onto stainless steel beads by adsorption followed by crosslinking, and onto polyacrylamide by covalent bonding. The activities of the two types of immobilized enzyme toward the particulate substrate, tributyrin emulsion droplets, were determined experimentally, and rate constants based on Michaelis‐Menten kinetics were calculated. The activity of the stainless steel–lipase was determined for various flow conditions and for various support sizes by the use of a differential fluidized bed recycle reactor. The rate constants calculated indicate that the experimental reaction rate is free from mass transfer influences, since the observed Michaelis constant does not vary with the fluidization velocity or with the support particle size. In addition, the Michaelis constant of the stainless steel–lipase was found to be equal to that of the free enzyme, suggesting that adsorption and subsequent crosslinking does not alter the enzyme–substrate affinity. The emulsion substrate mass transfer rates, calculated from the filtration theory, indicate that each substrate particle which contacts the immobilized enzyme is hydrolyzed to a significant extent. Theexperimentally determined kinetic rate constants may be used directly to predict the size of integral fluidized bed reactors.