Optimal covalent immobilization of α-chymotrypsin on Fe3O4-chitosan nanoparticles

Ju, Hen-Yi; Kuo, Chung‐Yih; Too, J. R.; Huang, Hsin‐Yi; Twu, Yawo-Kuo; Chang, Chieh-Ming J.; Liu, Yung-Chuan; Shieh, Chwen‐Jen

doi:10.1016/j.molcatb.2012.01.015

Cited by 39 publications

(10 citation statements)

References 34 publications

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“…This contrasts literature data for TiO 2 with anatase crystal structure, which has been found to inactivate chymotrypsin by oxidative damages at least after exposure to ultraviolet light [48,49]. In addition, autolysis of chymotrypsin, which has been reported to take place during incubations at around pH 8 [50][51][52], appears not to be involved in the observed loss of chymotrypsin activity from the supernatant, consistent with recently published data under similar conditions [53].…”

Section: Discussionsupporting

confidence: 77%

Physisorption of enzymatically active chymotrypsin on titania colloidal particles

Derr

Dringen

Treccani

et al. 2015

Journal of Colloid and Interface Science

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Section: Discussionsupporting

confidence: 77%

Physisorption of enzymatically active chymotrypsin on titania colloidal particles

Derr

Dringen

Treccani

et al. 2015

Journal of Colloid and Interface Science

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“…Ju et al covalently immobilized alpha‐chymotrypsin onto magnetic Fe 3 O 4 ‐chitosan nanoparticles. Optimal immobilization conditions were identified, under which the product yield catalyzed by immobilized enzyme was comparable to that of free enzyme and over 60% of the enzymatic activity was retained after using the system 12 times (Ju et al, ). It was shown that covalently immobilized glucose oxidase (GOX) on magnetite nanoparticles actually exhibited better enzymatic activity compared to free GOX in solution due to favorable conformational change of the enzyme (Rossi et al, ).…”

Section: Attachment Techniquesmentioning

confidence: 99%

Materials‐based strategies for multi‐enzyme immobilization and co‐localization: A review

Feng

Narasimhan

Mallapragada

2013

Biotech & Bioengineering

233

167

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Immobilized enzymes as biocatalysts have great potential both scientifically and industrially because of their technological and economic importance. Their highly efficient catalytic mechanisms and reusability have made them excellent candidates for green and sustainable applications. Previous studies have primarily focused on single enzyme immobilization. However, there are many situations where a single enzyme cannot completely catalyze reactions and multiple enzymes working together in a cascade are needed. It is very challenging to efficiently drive the multi-step reaction toward the desired direction, which is especially true when reactive intermediates are present. Nature overcomes this limitation through the use of multi-enzyme complexes (MECs) to promote the overall catalytic efficiency, which has inspired researchers to synthesize artificial MECs to controllably enhance the production of the desired compounds in multi-step reaction cascades in vitro. The most common approaches to synthesize artificial MECs are to use genetic engineering techniques to create fusion proteins or to co-localize multiple enzymes on suitable carriers. This review focuses on the latter with a particular emphasis on materials-based approaches to enzyme co-localization, which builds on techniques developed for single enzyme immobilization. The attachment techniques used in single enzyme immobilization are also effective in multiple enzyme co-localization, which has a direct impact on the overall enzyme orientation and activity. For carrier-based strategies, the platforms developed for single enzyme immobilization are also appropriate for attaching and co-localizing multiple enzymes. However, the involvement of multiple components in co-localization brings many challenges. The properties of different enzymes makes co-localization complicated when selecting attachment techniques and platforms to preserve enzymatic activity, because the structure and function of each component enzyme needs to be taken into consideration to preserve the overall enzyme activity. In addition, the relative position of the multiple enzymes in a confined space plays a significant role in the interactions between different enzymes, which makes spatial control important for co-localization. This review focuses on the potential of materials-based approaches for multiple enzyme co-localization for the design of sustainable multi-enzyme biocatalysts. A critical analysis of the attachment techniques and carriers platforms that have been used in enzyme immobilization and multi-enzyme co-localization in vitro is provided.

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“…It is of vital importance to select proper immobilization basis for protein immobilization. Fe 3 O 4 nanoparticles have been intensively utilized to realize this objective due to its unique magnetic performance, and various practical and economical biocatalysts with improved stability and reusability have been fabricated based on Fe 3 O 4 nanoparticles, which could be easily separated from the reaction medium in the presence of external magnetic field [1,2,3,4,5,6,7,8,9,10,95,96,97,98,99,100,101,102,103,104,105,106,107,108,109,110,111,112,113,114]. Proteins could be immobilized onto Fe 3 O 4 nanoparticles in the manner of physical absorption [95,96,97], covalent bonding [98,99,100,101,102,103,104], and bioconjugation [105,106,107].…”

Section: Applications Of Fe3o4 Nanoparticlesmentioning

confidence: 99%

Bio and Nanomaterials Based on Fe3O4

et al. 2014

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Abstract:During the past few years, nanoparticles have been used for various applications including, but not limited to, protein immobilization, bioseparation, environmental treatment, biomedical and bioengineering usage, and food analysis. Among all types of nanoparticles, superparamagnetic iron oxide nanoparticles, especially Fe3O4, have attracted a great deal of attention due to their unique magnetic properties and the ability of being easily chemical modified for improved biocompatibility, dispersibility. This review covers recent advances in the fabrication of functional materials based on Fe3O4 nanoparticles together with their possibilities and limitations for application in different fields.

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Optimal covalent immobilization of α-chymotrypsin on Fe3O4-chitosan nanoparticles

Cited by 39 publications

References 34 publications

Physisorption of enzymatically active chymotrypsin on titania colloidal particles

Physisorption of enzymatically active chymotrypsin on titania colloidal particles

Materials‐based strategies for multi‐enzyme immobilization and co‐localization: A review

Bio and Nanomaterials Based on Fe3O4

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