Use of novel immobilized β‐galactosidase reactor to hydrolyze the lactose constituent of skim milk
- 1 July 1990
- journal article
- research article
- Published by Wiley in Biotechnology & Bioengineering
- Vol. 36 (3) , 293-309
- https://doi.org/10.1002/bit.260360312
Abstract
β-galactosidase from Aspergillus oryzae immobilized in an axial-annular flow reactor was used to effect the hydrolysis of the lactose component of skim milk. Nonlinear regression methods were employed to determine the kinetic parameters of four rate expressions derived from a proposed enzymatic mechanism. Data taken at three different temperatures (30°C, 40°C, and 50°C) were fit via nonlinear regression methods assuming an Arrhenius temperature model for each of the parameters. For the reaction conditions used in this research, a three-parameter rate expression which includes the separate competitive inhibition effects of α- and β-galactose (and the associated mutarotation reaction) is sufficient to model the hydrolysis of lactose in skim milk. The effects of temperature on the individual kinetic parameters are small. The most significant effect appears in the term for inhibition by the β anomer of galactose (EA = 10.3 kcal/mol). At 40°C and a space time of 10 min, 70% of the lactose present in skim milk can be hydrolyzed with the axial-annular flow reactor. This reactor can be used to hydrolyze the lactose in skim milk without the problems observed with other reactor configurations, namely, plugging due to particulates, microbial contamination, and large pressure drop.Keywords
This publication has 25 references indexed in Scilit:
- Hydrolysis of lactose in skim milk by immobilized β‐galactosidase in a spiral flow reactorBiotechnology & Bioengineering, 1989
- The kinetic of lactose hydrolysis for the β‐galactosidase from Aspergillus nigerBiotechnology & Bioengineering, 1982
- Anatomy of a complex mutarotation. Kinetics of tautomerization of .alpha.-D-galactopyranose and .beta.-D-galactopyranose in waterJournal of the American Chemical Society, 1981
- A quantitation of the factors which affect the hydrolase and transgalactosylase activities of β-galactosidase (E. coli) on lactoseBiochemistry, 1976
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Beta‐galactosidase technology: A solution to the lactose problemC R C Critical Reviews in Food Technology, 1975
- Hydrolysis of ?-galactosides using polymer-entrapped lactase. A study towards producing lactose-free milkBiotechnology & Bioengineering, 1973
- The kinetics of β‐galactosidase attached to porous cellulose sheetsBiotechnology & Bioengineering, 1969
- Preparation and Use of Porous Sheets with Enzyme ActionNature, 1968
- A Schematic Method of Deriving the Rate Laws for Enzyme-Catalyzed ReactionsThe Journal of Physical Chemistry, 1956