Improving and Tailoring Enzymes for Food Quality and Functionality
11 - Enzyme engineering (immobilization) for food applications
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Designing multifunctional biocatalytic cascade system by multi-enzyme co-immobilization on biopolymers and nanostructured materials
2023, International Journal of Biological MacromoleculesCitation Excerpt :Recently, the focus has been directed to carrying out enzymatic reactions closer to industrial settings, and such conditions necessitate bioprocessing performance metrics far from those observed in the laboratory. To achieve this, evaluation of biocatalytic activity (U/L), specific activity (U/mg enzyme), mass activity (U/g carrier), biocatalytic product yield (g product/g biocatalyst), productivity (g product/L reactor per hour), product concentration (g product/L reactor) and yield of product on the substrate (g product/g substrate) could be considered valuable to benchmark bioprocesses and set goals for further developments [24]. Carrier-based immobilization techniques involve attaching enzyme molecules to or confinement within a solid carrier.
Highly efficient removal of patulin using immobilized enzymes of Pseudomonas aeruginosa TF-06 entrapped in calcium alginate beads
2022, Food ChemistryCitation Excerpt :Consequently, preventing the conversion of ascladiol to patulin or promoting the biodegradation of patulin to nontoxic ascladiol should be effective strategies for the reduction of patulin toxicity (Tannous et al., 2017). As an internationally accepted food additive, calcium alginate has been widely used for enzyme immobilization for purpose of increasing the application performance of free enzymes in food industry (Agyei et al., 2015; Qin, Jiang, Zhao, Zhang, & Wang, 2018). Previous works indicated that immobilization of pectinmethylesterase and tannase using calcium alginate could offer many advantages over free enzymes, including high activity, increasing thermal and pH stability and the easy separation from the final product (Bogra, Kumar, Kuhar, Panwar, & Singh, 2013; De Lima et al., 2018).
Improvement of enzymatic performance of Asclepias curassavica L. proteases by immobilization. Application to the synthesis of an antihypertensive peptide
2020, Process BiochemistryCitation Excerpt :The design of reaction media and the determination of the best biocatalyst configuration are major challenges for peptide synthesis, since proteases, different from lipases, are not structurally conditioned to act in such environments [1,3]. Enzyme immobilization is a powerful strategy for the preparation of biocatalysts with improved properties that allows increasing the efficiency of catalyst use with the consequent impact on process cost savings [6,7]. Enzyme immobilization allows biocatalyst recovery and reuse, so that several production cycles can be carried out without biocatalyst replenishment and long-term continuous processes can be developed [8].