scholarly journals Optimization of enzyme immobilization on magnetic microparticles using 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) as a crosslinking agent

2015 ◽  
Vol 7 (24) ◽  
pp. 10291-10298 ◽  
Author(s):  
F. Kazenwadel ◽  
H. Wagner ◽  
B. E. Rapp ◽  
M. Franzreb

Enzyme immobilization is a versatile tool in biotransformation processes to enhance enzyme activity and to secure an easy separation of catalysts and products and the reusability of enzymes.

2019 ◽  
Vol 25 (24) ◽  
pp. 2661-2676 ◽  
Author(s):  
Sundaresan Bhavaniramya ◽  
Ramar Vanajothi ◽  
Selvaraju Vishnupriya ◽  
Kumpati Premkumar ◽  
Mohammad S. Al-Aboody ◽  
...  

Enzymes exhibit a great catalytic activity for several physiological processes. Utilization of immobilized enzymes has a great potential in several food industries due to their excellent functional properties, simple processing and cost effectiveness during the past decades. Though they have several applications, they still exhibit some challenges. To overcome the challenges, nanoparticles with their unique physicochemical properties act as very attractive carriers for enzyme immobilization. The enzyme immobilization method is not only widely used in the food industry but is also a component methodology in the pharmaceutical industry. Compared to the free enzymes, immobilized forms are more robust and resistant to environmental changes. In this method, the mobility of enzymes is artificially restricted to changing their structure and properties. Due to their sensitive nature, the classical immobilization methods are still limited as a result of the reduction of enzyme activity. In order to improve the enzyme activity and their properties, nanomaterials are used as a carrier for enzyme immobilization. Recently, much attention has been directed towards the research on the potentiality of the immobilized enzymes in the food industry. Hence, the present review emphasizes the different types of immobilization methods that is presently used in the food industry and other applications. Various types of nanomaterials such as nanofibers, nanoflowers and magnetic nanoparticles are significantly used as a support material in the immobilization methods. However, several numbers of immobilized enzymes are used in the food industries to improve the processing methods which not only reduce the production cost but also the effluents from the industry.


Author(s):  
Maria Laura Soriano

A new tendency toward the design of artificial enzymes based on nanostructures (nanodots, nanofibers, mesoporous materials) has emerged. On one hand, nanotechnology bestows self-catalytic nanoparticles with a specific activity to achieve efficient reactions with low number of by-products. On other hand, the nanoparticles may behave as nanometric scaffolds for hosting enzymes, promoting their catalytic activity and stability. In this case, enzyme immobilization requires the preservation of the catalytic activity by preventing enzyme unfolding and avoiding its aggregation. These approaches render many other advantages like hosting/storing enzymes in nanotechnological solid, liquid, and gel-like media. This chapter focuses on the most up-to-date approaches to manipulate or mimic enzyme activity based on nanotechnology, and offers examples of their applications in the most promising fields. It also gives new insight into the creation of reusable nanotechnological tools for enzyme storage.


RSC Advances ◽  
2014 ◽  
Vol 4 (4) ◽  
pp. 1583-1600 ◽  
Author(s):  
Oveimar Barbosa ◽  
Claudia Ortiz ◽  
Ángel Berenguer-Murcia ◽  
Rodrigo Torres ◽  
Rafael C. Rodrigues ◽  
...  

ChemInform ◽  
2014 ◽  
Vol 45 (21) ◽  
pp. no-no ◽  
Author(s):  
Oveimar Barbosa ◽  
Claudia Ortiz ◽  
Angel Berenguer-Murcia ◽  
Rodrigo Torres ◽  
Rafael C. Rodrigues ◽  
...  

2016 ◽  
Vol 52 (66) ◽  
pp. 10159-10162 ◽  
Author(s):  
Joshua Britton ◽  
Colin L. Raston ◽  
Gregory A. Weiss

Continuous flow biocatalysis gets a new spin. An efficient and general enzyme immobilization technique for vortex fluidic processing has been developed. The immobilized enzyme demonstrated no decrease in enzyme activity over 10 h in continuous flow with a >95% reduction in quantities of required reagents and enzymes.


Author(s):  
Leila Yavari Maroufi ◽  
Mohsen Rashidi ◽  
Mahnaz Tabibiazar ◽  
Maryam Mohammadi ◽  
Akram Pezeshki ◽  
...  

Enzymes are one of the main biocatalysts with various applications in the food industry. Stabilization of enzymes on insoluble carriers is important due to the low reuse, low operational stability, and high cost in applications. The immobility and the type of carrier affect the activity of the immobile enzyme. Hydrogels are three-dimensionally cross-linked macromolecular network structures designed from various polymers. Hydrogels can provide a matrix for an immobile enzyme due to their extraordinary properties such as high water absorbing capacity, carrier of bioactive substances and enzymes, biocompatibility, safety, and biodegradability. Therefore, this study mainly focuses on some enzymes (Lactase, Lipases, Amylases, Pectinase, Protease, Glucose oxidase) that are of special importance in the food industry. These enzymes could be immobilized in the hydrogels constructed of macromolecules such as kappa-carrageenan, chitosan, arabic gum, pectin, alginate, and cellulose. At last, in the preparation of these hydrogels, different enzyme immobilization methods in macromolecular hydrogels, and effect of hydrogels on enzyme activity were discussed.


2019 ◽  
Vol 7 (7) ◽  
pp. 2841-2849 ◽  
Author(s):  
Di Li ◽  
Zheng Fang ◽  
Hongwei Duan ◽  
Li Liang

Constructing calcium phosphate (CaP)–gold (Au) nanocomposites for enzyme immobilization to overcome the bottleneck of loss of enzyme activity upon immobilization.


Small ◽  
2019 ◽  
Vol 15 (20) ◽  
pp. 1970104
Author(s):  
Samuel Lim ◽  
Gi Ahn Jung ◽  
Dominic J. Glover ◽  
Douglas S. Clark

SynOpen ◽  
2018 ◽  
Vol 02 (02) ◽  
pp. 0192-0199 ◽  
Author(s):  
A. Grollmisch ◽  
U. Kragl ◽  
J. Großeheilmann

Enzyme immobilization in polymerized ionic liquids (PILs) promises to be a versatile tool for simple recovery and reuse of catalysts. In this study, a raw extract of CalB was encapsulated in poly(VEImBr) and assessed with respect to solvent, temperature, amount of enzyme, leaching behavior, and reusability on the example of the kinetic resolution of rac-1-phenylethanol with vinyl acetate. This immobilization method increased the enzyme activity of the CalB raw extract in comparison to the non-immobilized enzyme. The desired product was synthesized with high enantiomeric excess (ee) and no leaching of active enzyme was observed in the experiments. The immobilization method was compared to Novozyme 435 and Lipozyme RM IM, as commercially available immobilisates. Nonpolar solvents, including n-heptane and n-dodecane, proved to be the best reaction solvents, showing nearly full conversion and high catalytic activities. The encapsulated ­lipase was easily recovered from the reaction mixture and reused for ten cycles.


Author(s):  
S.M. Geyer ◽  
C.L. Mendenhall ◽  
J.T. Hung ◽  
E.L. Cardell ◽  
R.L. Drake ◽  
...  

Thirty-three mature male Holtzman rats were randomly placed in 3 treatment groups: Controls (C); Ethanolics (E); and Wine drinkers (W). The animals were fed synthetic diets (Lieber type) with ethanol or wine substituted isocalorically for carbohydrates in the diet of E and W groups, respectively. W received a volume of wine which provided the same gram quantity of alcohol consumed by E. The animals were sacrificed by decapitation after 6 weeks and the livers processed for quantitative triglycerides (T3), proteins, malic enzyme activity (MEA), light microscopy (LM) and electron microscopy (EM). Morphometric analysis of randomly selected LM and EM micrographs was performed to determine organellar changes in centrilobular (CV) and periportal (PV) regions of the liver. This analysis (Table 1) showed that hepatocytes from E were larger than those in C and W groups. Smooth endoplasmic reticulum decreased in E and increased in W compared to C values.


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