Staff Members - Benha University
Ultrasound assisted enzymolysis of sunflower meal protein: Kinetics and thermodynamics modeling
Journal of Food Process Engineering • 2018
Publication Information
Authors
Mokhtar Dabbour; Ronghai He; Benjamin Mintah; Yingxiu Tang; Haile Ma
Keywords
Not Available
Journal
Journal of Food Process Engineering
Publisher
wiley
Volume
Not Available
Issue
Not Available
Pages
Not Available
publication.type
International
Paper Link
Open Link
Supplementary Materials
Not Available
Abstract
This study examined the effect of dual-frequency ultrasound (DFU) pretreatment on thermodynamics
and kinetics of sunflower-meal protein (SMP) using alcalase to improve efficiency in
enzymolysis process. The concentration of hydrolyzed protein and kinetic parameters after traditional
pretreatment (control) were investigated and compared with DFU-assisted enzymolysis.
The results indicated that DFU-pretreatment enhanced SMP-enzymolysis efficiency at different
substrate and enzyme concentrations, temperature, and pH. Kinetics analysis showed DFUpretreatment
reduced the Michaelis constant by 11.29%, while the apparent breakdown rate
constant increased by 1.96%, indicating DFU-pretreatment improved the affinity among substrate
and enzyme. The rate constants for DFU-pretreatment were increased by 45.96, 26.92,
21.14, and 27.89% at 293, 303, 313, and 323 K, respectively (p < .05). On Arrhenius kinetics,
DFU reduced the activation energy, enthalpy and entropy by 24.28, 26.13, and 9.10%, respectively
(p < .05). DFU had slight influence on Gibbs-free energy when temperature increased
from 293 to 323 K.
and kinetics of sunflower-meal protein (SMP) using alcalase to improve efficiency in
enzymolysis process. The concentration of hydrolyzed protein and kinetic parameters after traditional
pretreatment (control) were investigated and compared with DFU-assisted enzymolysis.
The results indicated that DFU-pretreatment enhanced SMP-enzymolysis efficiency at different
substrate and enzyme concentrations, temperature, and pH. Kinetics analysis showed DFUpretreatment
reduced the Michaelis constant by 11.29%, while the apparent breakdown rate
constant increased by 1.96%, indicating DFU-pretreatment improved the affinity among substrate
and enzyme. The rate constants for DFU-pretreatment were increased by 45.96, 26.92,
21.14, and 27.89% at 293, 303, 313, and 323 K, respectively (p < .05). On Arrhenius kinetics,
DFU reduced the activation energy, enthalpy and entropy by 24.28, 26.13, and 9.10%, respectively
(p < .05). DFU had slight influence on Gibbs-free energy when temperature increased
from 293 to 323 K.