Immobilization and Biochemical Characterization of Keratinase 2S1 onto Magnetic Cross-Linked Enzyme Aggregates and its Application on the Hydrolysis of Keratin Waste

Lotfi, Fatemeh; Badoei-dalfard, Arastoo; Hassanshahian, Mehdi

doi:10.1007/s10562-021-03833-z

Cited by 5 publications

(3 citation statements)

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“…Lofti et al immobilized purified keratinase 2S1 in the form of cross-linked aggregates (CLEA) bound to pretreated magnetic Fe 3 O 4 nanoparticles and found that the V max of immobilized keratinase was 7.96-fold greater than that of free keratinase. Additionally, the thermal stability of immobilized keratinase was improved by 3.5-fold and 5.8-fold after 3 h of incubation at 70 and 80 °C, respectively . However, noncovalent immobilization is a relatively weak interaction.…”

Section: Eximious Approaches For Enhancing the Catalytic Capacity Of ...mentioning

confidence: 99%

“…Additionally, the thermal stability of immobilized keratinase was improved by 3.5-fold and 5.8fold after 3 h of incubation at 70 and 80 °C, respectively. 82 However, noncovalent immobilization is a relatively weak interaction. As a result, proteins are easily detached from the carrier, which leads to the enzyme becoming inactive again when it has been restored to its free state.…”

Section: Modification Of Thermostabilitymentioning

confidence: 99%

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Perspective on Agricultural Industrialization: Modification Strategies for Enhancing the Catalytic Capacity of Keratinase

Yan,

Chen,

Feng

et al. 2024

J. Agric. Food Chem.

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Keratinases is a special hydrolytic enzyme produced by microorganisms, which has the ability to catalyze the degradation of keratin. Currently, keratinases show great potential for application in many agricultural and industrial fields, such as biofermented feed, leather tanning, hair removal, and fertilizer production. However, these potentials have not yet been fully unleashed on an industrial scale. This paper reviews the sources, properties, and catalytic mechanisms of keratinases. Strategies for the molecular modification of keratinases are summarized and discussed in terms of improving the substrate specificity, thermostability, and pH tolerance of keratinases. The modification strategies are also enriched by the introduction of immobilized enzymes and directed evolution. In addition, the selection of modification strategies when facing specific industrial applications is discussed and prospects are provided. We believe that this review serves as a reference for the future quest to extend the application of keratinases from the laboratory to industry.

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Section: Eximious Approaches For Enhancing the Catalytic Capacity Of ...mentioning

confidence: 99%

Section: Modification Of Thermostabilitymentioning

confidence: 99%

Perspective on Agricultural Industrialization: Modification Strategies for Enhancing the Catalytic Capacity of Keratinase

Yan,

Chen,

Feng

et al. 2024

J. Agric. Food Chem.

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“…Industrial application of mCLEAs and m-combi-CLEAs has the possibility of using them in the complex conversions of polysaccharides such as starch (Torabizadeh and Montazeri, 2020), lignocellulose for the production of firstand second-generation biofuels (Cruz-Izquierdo et al, 2015), for the synthesis of bioactive molecules as aglycone (Wei et al, 2022), and for clarification and flavor enhancers in food and beverages (Dal Magro et al, 2018). Likewise, magnetic CLEAs can be used in the conversion of biomass as in the valorization of keratin-rich poultry industry wastes where keratinase m-CLEA showed enhanced activity and stability than the soluble enzyme (Lotfi et al, 2021), as well as in the enantioselective reduction of prochiral ketones catalyzed by magnetic combi-CLEAs of his-tagged ketoreductase and histagged glucose oxidase (Peschke et al, 2019), for dyedegradation in wastewater (Wang et al, 2021). New CLEAs for industrial applications have gained prominence in this context since they generate correct environmental products and sustainable chemical systems.…”

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confidence: 99%

Editorial: Designing Carrier-Free Immobilized Enzymes for Biocatalysis

Velasco‐Lozano

Rocha-Martín

Santos

2022

Front. Bioeng. Biotechnol.

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Editorial on the Research TopicDesigning Carrier-free Immobilized Enzymes for Biocatalysis Global challenges in energy, resources, environment and sustainable chemical processing are leading us to minimize the use of natural resources, toxic materials, energy, and the generation of waste and pollutants. Enzymatic biocatalysis development evolves to strengthen the ongoing required process improvements of current industrial chemical transformations, where enzymes are naturally available, efficient biocatalysts exhibiting high specificity and enantioselectivity. However, for their industrial application, enzymes must possess high stability under large-scale producing conditions (such as high substrate and product concentrations, temperature, presence of solvents), where enzymes easily become inactive due to their low stability under such unnatural conditions or the almost null activity toward non-natural substrates. In this context, enzyme immobilization is a strategy that can facilitate their stabilization, purification, and reuse in the industry (Cavalcante et al., 2021; da S. Moreira et al., 2021;Reis et al., 2019). Enzymes can be immobilized on water-insoluble supports or without supports. Among carrier-free immobilization methods, the Cross-Linked Enzyme Aggregates (CLEA) emerged as a promising technology capable of manufacturing robust immobilized protein aggregates. In general, the preparation of CLEA involves the first stage of precipitation of enzymatic molecules followed by a cross-linking step managed by the action of a bifunctional reagent added to the reaction system, the cross-linker. As a result, the aggregates become insoluble, maintaining high catalytic activity, excellent stability, and low production cost.Another possibility of immobilizing enzymes free of support is the cross-linked enzyme crystals (CLEC). Compared to soluble enzymes, CLEC is more robust, controllable in size, resistant to organic solvents, and inactivates by heat or proteolysis. However, in contrast with CLEA, CLEC requires purified enzymes to achieve the required enzyme crystals formation, thus hampering their implementation at significant scale processes.CLEAs's physical and catalytic properties are strongly influenced and controlled through the preparation process (Table 1). Several works have summarized the most reported variables leading to robust CLEA biocatalysts from a wide variety of different enzymes, such as hydrolases, oxidoreductases, lyases, transferases, and isomerases for different industrial applications (Talekar

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