The aim of this study was to carry out the co-immobilization of α-amylase and glucoamylase in crosslinked gelatin porous supports. For this, two methods of co-immobilization were proposed based on the crosslinking with glutaraldehyde (Ggta) or CaCl in presence of alginate (Gcal). The supports characterization revealed a porous microstructure with good interaction between its components according to the FTIR analysis and thermal properties. Optimal pH and temperature of the Gcal co-immobilized enzymes were determined at 60 °C and pH 6.0, present an enzymatic activity of 120 μmol·mL·min. Moreover, both supports were reused for up to 8 hydrolysis cycles. In addition, co-immobilized enzymes were more efficient than free enzymes in starch saccharification of starch in the long term. These results reveal that the co-immobilization of amylases in gelatinous supports is a promising approach in enzymatic chain reactions.
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http://dx.doi.org/10.1016/j.ijbiomac.2020.09.220 | DOI Listing |
Food Chem
July 2024
Kweichow Moutai Group, Renhuai, Guizhou 564501, China; Guizhou Key Laboratory of Microbial Resources Exploration in Fermentation Industry, Kweichow Moutai Group, Zunyi 564501, China. Electronic address:
Multiple enzymes induce biological cascade catalysis is essential in nature and industrial production. However, the shortcomings of enzymes, including unsatisfactory stability, reusability, and sensitivity in harsh microenvironment, have restricted their broader use. Here, we report a facile method for fabricating a cascade system by combining the benefits of immobilized enzymes and biomimetic catalysis based on magnetic metal-organic framework nanoflowers (mMOFNFs).
View Article and Find Full Text PDFEnzyme Microb Technol
October 2023
Departamento de Engenharia Química, Universidade Federal do Rio Grande do Norte, Natal, RN, Brazil. Electronic address:
This review emphasizes the crucial role of enzyme immobilization technology in advancing the production of two main biofuels, ethanol and biodiesel, with a specific focus on the Cross-linked Enzyme Aggregates (CLEAs) strategy. This method of immobilization has gained attention due to its simplicity and affordability, as it does not initially require a solid support. CLEAs synthesis protocol includes two steps: enzyme precipitation and cross-linking of aggregates using bifunctional agents.
View Article and Find Full Text PDFBiomed Chromatogr
March 2023
School of Light Industry and Chemical Engineering, Dalian Polytechnic University, Dalian, China.
Morus alba leaves are a natural product with great antidiabetic potential. However, the therapeutic efficacy of natural products is usually achieved through the interaction of active compounds with specific targets. Among them, active compounds with multi-target therapeutic functions are more effective than single-target enzymes.
View Article and Find Full Text PDFFood Chem
January 2023
University of Hatay Mustafa Kemal, Faculty of Arts & Sciences, Department of Chemistry, 31040 Hatay, Turkey.
In this study, the use of co-immobilized amylase, pectinase and cellulase enzymes for clarification of apple, grape and pear juices were investigated. Four different co-immobilization method was applied and the highest activity was observed for co-immobilized enzymes onto silica gel. The effect of the enzyme units used in the co-immobilization, reaction temperature and time on turbidity and reducing sugar concentration were optimized by Response Surface Methodology (RSM) via Design Expert Software 8.
View Article and Find Full Text PDFFood Chem
December 2021
Department of Food Science, University of Massachusetts, Amherst, MA 01003, United States. Electronic address:
Anthocyanins, which are natural pigments and nutraceuticals, can be extracted from plant materials using enzyme-assisted methods. However, the enzymes used are often expensive, fragile, and hard to recover/reuse. In this study, cellulase and α-amylase were immobilized on amino-functionalized magnetic nanoparticles to prepare a magnetic nanobiocatalyst.
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