Luffa cylindrica sponges as a thermally and chemically stable support for Aspergillus niger lipase

Abstract

The use of biopolymer compounds as matrices for enzyme immobilization is currently a focus of increasing interest. In the present work we propose the use of Luffa cylindrica vegetable sponges as a support for the lipase extracted from Aspergillus niger. Effectiveness of immobilization was analyzed using Fourier transform infrared spectroscopy, elemental analysis and the Bradford method. An initial enzyme solution concentration of 1.0 mg/mL and an immobilization time of 12 h were selected as the parameters that produce a system retaining the highest hydrolytic activity (84% of free enzyme). The resulting biocatalyst system also exhibited high thermal and chemical stability, reusability and storage stability, which makes it a candidate for use in a wide range of applications. Kinetic parameters for the native and immobilized lipase were also calculated. The value of the Michaelis-Menten constant for the immobilized lipase (0.47 mM) is higher than for the free enzyme (0.21 mM), which indicates that the adsorbed enzyme exhibits a lower affinity to the substrate than native lipase. © 2016 American Institute of Chemical Engineers Biotechnol. Prog., 32:657-665, 2016.

Spongin-Based Scaffolds from Hippospongia communis Demosponge as an Effective Support for Lipase Immobilization

“…Catalysts 2017, 7, 147 4 of 19 [32,33]. SEM images taken after enzyme immobilization (process parameters: 2 h process duration, 4 °C, pH 7) confirmed the successful deposition of the lipase by the presence of enzyme aggregates on the surface of the spongin fibers, as mentioned previously [34]. These results are confirmed by observations from digital microscopy (Figure 1e,f).…”

“…The marine keratosan demosponges exhibit a three-dimensional open network structure built from similar, branched spongin fibers with a slightly corrugated surface at a diameter of 20 μm The marine keratosan demosponges exhibit a three-dimensional open network structure built from similar, branched spongin fibers with a slightly corrugated surface at a diameter of 20 µm [32,33]. SEM images taken after enzyme immobilization (process parameters: 2 h process duration, 4 • C, pH 7) confirmed the successful deposition of the lipase by the presence of enzyme aggregates on the surface of the spongin fibers, as mentioned previously [34]. These results are confirmed by observations from digital microscopy (Figure 1e,f).…”

A General Overview of Support Materials for Enzyme Immobilization: Characteristics, Properties, Practical Utility

“…As reported by Kim et al cellulose nanocrystals obtained from cotton linter cellulose can be used for immobilization by non-specific adsorption interactions of Candida rugosa lipase with high loading efficiency [65], whilst lipase was immobilized by entrapment by Tumturk et al using κ-carrageenan hydrogels [66]. Vegetable and marine sponges characterized by an open fibrous network that reduces diffusional limitations have also been used as matrices for the immobilization of lipases, mainly via hydrogen bonds [67,68]. It may be concluded that biopolymers can be used to immobilize enzymes belonging to various catalytic classes with the retention of good catalytic properties.…”

3D Chitin Scaffolds from the Marine Demosponge Aplysina archeri as a Support for Laccase Immobilization and Its Use in the Removal of Pharmaceuticals

“…For this reason, interference in the structure of the enzyme and its distortion upon immobilization are limited [57]. This is a possible explanation of the high specific activity of the immobilized laccase (52.5 U/mg) as compared to the free enzyme (56 U/mg), corresponding to an activity retention of 89% [58]. By contrast, Das et al immobilized laccase on magnetic iron nanoparticles and obtained specific activity of the immobilized protein was about 15 U/mg, that was almost two times lower as compared to free laccase (30 U/mg) [59].…”