• Citations Citations 37
• References References 52

• particles. Haupt et al. demonstrated that whenever glucoamylase and b-glucosidase were individually immobilized on polyelectrolyte brushes of poly (acrylic acidity) or poly(styrene sulfonic acidity)-polystyrene based core–shell nanoparticles, the enzymes could maintain activity and loading efficiencies up to 600 mg/g were achieved (Haupt et al. 2005). Mileti et al. (2010) immobilized Candida antarctica lipase on polystyrene nanoparticles by adsorption. A higher loading efficiency of 240 mg/g was reported, separate from pH. The merchandise performance was better than those of the crude enzyme powder and commercial novozyme 435. For multi-enzyme co-localization. in Watanabe&#x27s work, Pain, choline oxidase, and HR

[Show abstract] [Hide abstract] ABSTRACT: Immobilized enzymes as biocatalysts have great potential both scientifically and industrially due to their technological and economic importance. Their highly efficient catalytic mechanisms and reusability make them excellent candidates for eco-friendly and sustainable applications. Previous research has mainly centered on single enzyme immobilization. However, there are lots of situations in which a single enzyme cannot completely catalyze reactions and multiple enzymes cooperating inside a cascade are essential. It’s very difficult to efficiently drive the multi-step reaction toward the preferred direction, that is particularly true when reactive intermediates can be found. Nature overcomes this limitation by using multi-enzyme complexes (MECs) to advertise the general catalytic efficiency, that has inspired researchers to synthesize artificial MECs to controllably enhance producing the preferred compounds in multi-step reaction cascades in vitro.

The most typical methods to synthesize artificial MECs will be to use genetic engineering strategies to create fusion proteins in order to co-localize multiple enzymes on appropriate carriers. This review concentrates on the second having a particular focus on materials-based methods to enzyme co-localization, which develops techniques produced for single enzyme immobilization. The attachment approaches single enzyme immobilization will also be good at multiple enzyme co-localization, with a direct effect on the general enzyme orientation and activity. For carrier-based strategies, the platforms produced for single enzyme immobilization will also be suitable for attaching and co-localizing multiple enzymes. However, the participation of multiple components in co-localization brings many challenges. The qualities of various enzymes makes co-localization complicated when choosing attachment techniques and platforms to preserve enzymatic activity, since the structure and performance of every component enzyme must be considered to preserve the general enzyme activity. Additionally, the relative position from the multiple enzymes inside a limited space plays a substantial role within the interactions between different enzymes, making spatial control essential for co-localization. This review concentrates on the potential for materials-based methods for multiple enzyme co-localization for the style of sustainable multi-enzyme biocatalysts.

A vital research into the attachment techniques and carriers platforms which have been utilized in enzyme immobilization and multi-enzyme co-localization in vitro is supplied. Biotechnol. Bioeng. 2013 Wiley Periodicals, Corporation.

Full-text · Article · February 2014

Feng Jia Balaji Narasimhan Surya Mallapragada

• Besides, the rest of the metals in the conventional catalysts are difficult to get rid of, which might cause undesirable pollution upon disposal [12]. Candida antarctica Lipase B (CALB) is an extremely versatile biocatalyst for polyester synthesis, dealing with various monomers and organic solvents under mild conditions [12,1415161718192021222324252627. CALB-catalyzed synthesis of polyesters from eco-friendly monomers has lately acquired growing recognition.

[Show abstract] [Hide abstract] ABSTRACT: Bio-based commercially accessible succinate, itaconate and 1,4-butanediol are enzymatically co-polymerized in solution using a two-stage method, using Candida antarctica Lipase B (CALB, in immobilized form as Novozyme® 435) because the biocatalyst. Caffeine structures from the acquired products, poly(butylene succinate) (PBS) and poly(butylene succinate-co-itaconate) (PBSI), are confirmed by 1H- and 13C-NMR. The results from the reaction conditions around the CALB-catalyzed synthesis of PBSI are fully investigated, and also the optimal polymerization the weather is acquired. Using the established method, PBSI with tunable compositions and satisfying reaction yields is created. The 1H-NMR results make sure carbon-carbon double bonds are very well preserved in PBSI. The differential checking calorimetry (DSC) and thermal gravimetric analysis (TGA) results indicate that the quantity of itaconate within the co-polyesters doesn’t have apparent effects around the glass-transition temperature and also the thermal stability of PBS and PBSI, but has significant effects around the melting temperature.

Full-text · Article · Sep 2013

Yi Jiang Albert J J Woortman Gert O R Alberda van Ekenstein Katja Loos

• The buffer pH 9. supported relatively high immobilization percentage because the enzyme conformation that is vital for enzymatic activity, changes using the pH. Further, the lower immobilization efficiency observed at low pH are closely related for an unfavorable charge distribution around the amino acidity residues that created an additional decrease activity [26]. Thus, the buffer of pH 9. was selected and used out of all subsequent experiments of immobilization.

[Show abstract] [Hide abstract] ABSTRACT: A manuscript and straightforward method was created for that preparation of magnetic Fe3O4 nanoparticles by chemical co-precipitation method and subsequent coating with 3-aminopropyltrimethoxysilane (APTMS) through silanization process. Magnetic Fe3O4-chitosan particles were made by the suspension mix-linking and covalent technique for use in the use of magnetic carrier technology. The synthesized immobilization supports were characterised by checking electron microscopy (SEM), thermogravimetric analysis (TGA) and X-ray diffraction (XRD). Using glutaraldehyde because the coupling agent, the lipase from R. oryzae was effectively immobilized to the functionalized magnetic Fe3O4-chitosan beads. The outcomes demonstrated that 86.60% of R. oryzae lipase was bound around the synthesized immobilization support. This immobilized lipase was effectively employed for the esterification of phenolic acidity which led to esterification of phenolic acidity in isooctane solvent reaction system for 8 consecutive cycles (totally 384 h), 72.6% of their initial activity was retained, indicating a higher stability in pharmaceutical and industrial applications. 2013 The Korean Society for Biotechnology and Bioengineering and Springer-Verlag Berlin Heidelberg.

Full-text · Article · August 2013