Date of Defense
26-11-2024 11:30 AM
Location
F3-040
Document Type
Thesis Defense
Degree Name
Master of Science in Chemical Engineering (MSChE)
College
College of Engineering
Department
Chemical and Petroleum Engineering
First Advisor
Prof. Sulaiman Al-Zuhair
Keywords
Alcalase; Protein hydrolysis; Zeolitic imidazolate framework; Kinetics modelling; Bioactive peptides
Abstract
This thesis aims to explore the use of Zeolitic Imidazolate Framework-L (ZIF-L) as a support for immobilizing alcalase and its potency in producing protein hydrolysates. ZIF-L was synthesized at room temperature using an aqueous solution, and alcalase was immobilized through adsorption batch experiment. The successful immobilization of alcalase on ZIF-L was confirmed through Fourier-transform infrared spectroscopy (FTIR), X-ray diffraction (XRD), scanning electron microscopy (SEM), and thermogravimetric analysis (TGA). The maximum adsorption capacity of alcalase on ZIF-L was determined to be 672.1 ± 5.5 mg g-1 at 40°C using an initial protein concentration of 5 mg mL-1. Adsorption equilibrium data suggested that alcalase physically adsorbed on ZIF-L, with the Freundlich model isotherm model providing the best fit. The adsorption kinetics were well described by pseudo-first order model, indicating that both film and intraparticle diffusion were significant. The activity of the prepared immobilized alcalase on ZIF-L was tested using bovine serum albumin as a substrate. Impressively, the immobilized alcalase retained over 90% of the initial activity after being stored at 4 °C for up to 70 days. A diffusion–reaction model was developed and numerically solved to describe the reaction dynamics, revealing the significance of mass transfer limitations during the early stages of hydrolysis. Furthermore, the immobilized alcalase was used to hydrolyse protein extracted from microalgae, and the bioactivity of the resulting peptides assessed through total phenolic content and radical scavenging activity assays. The findings underscore the potential of alcalase-based biocatalysts immobilized on ZIF-L for applications in food industry, offering a sustainable and cost-effective approach to producing bioactive peptides with health-promoting properties. This research opens avenues for further exploration of MOF-based enzyme immobilization in various biotechnological applications.
Included in
KINETICS, THERMODYNAMICS, AND BIOLOGICAL CHARACTERIZATIONS OF HYDROLYSATES ENZYMATICALLY PRODUCED FROM PROTEINS EXTRACTED FROM MICROALGAE
F3-040
This thesis aims to explore the use of Zeolitic Imidazolate Framework-L (ZIF-L) as a support for immobilizing alcalase and its potency in producing protein hydrolysates. ZIF-L was synthesized at room temperature using an aqueous solution, and alcalase was immobilized through adsorption batch experiment. The successful immobilization of alcalase on ZIF-L was confirmed through Fourier-transform infrared spectroscopy (FTIR), X-ray diffraction (XRD), scanning electron microscopy (SEM), and thermogravimetric analysis (TGA). The maximum adsorption capacity of alcalase on ZIF-L was determined to be 672.1 ± 5.5 mg g-1 at 40°C using an initial protein concentration of 5 mg mL-1. Adsorption equilibrium data suggested that alcalase physically adsorbed on ZIF-L, with the Freundlich model isotherm model providing the best fit. The adsorption kinetics were well described by pseudo-first order model, indicating that both film and intraparticle diffusion were significant. The activity of the prepared immobilized alcalase on ZIF-L was tested using bovine serum albumin as a substrate. Impressively, the immobilized alcalase retained over 90% of the initial activity after being stored at 4 °C for up to 70 days. A diffusion–reaction model was developed and numerically solved to describe the reaction dynamics, revealing the significance of mass transfer limitations during the early stages of hydrolysis. Furthermore, the immobilized alcalase was used to hydrolyse protein extracted from microalgae, and the bioactivity of the resulting peptides assessed through total phenolic content and radical scavenging activity assays. The findings underscore the potential of alcalase-based biocatalysts immobilized on ZIF-L for applications in food industry, offering a sustainable and cost-effective approach to producing bioactive peptides with health-promoting properties. This research opens avenues for further exploration of MOF-based enzyme immobilization in various biotechnological applications.