Chemical and physical Chitosan modification for designing enzymatic industrial biocatalysts: How to choose the best strategy?

Nunes, Yale Luck; Menezes, Fernando Lima de; Sousa, Isamayra Germano de; Cavalcante, Antônio Luthierre Gama; Cavalcante, Francisco Sales Ávila; Moreira, Katerine da Silva; Oliveira, André Luiz Barros de; Mota, Gabrielly Ferreira; Souza, José Erick da Silva; Falcão, Ítalo Rafael de Aguiar; Rocha, Thales Guimarães; Valério, Roberta Bussons Rodrigues; Fechine, Pierre Basílio Almeida; Souza, Monique; Santos, José Cleiton Sousa dos

doi:10.1016/j.ijbiomac.2021.04.004

Cited by 106 publications

(39 citation statements)

References 778 publications

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“…In addition, immobilization prevented lipase release and improved the stability of the three-dimensional structure. 14,15 Moreover, immobilizaiton is also an efficient way to purify enzymes, especially for lipases. 16 Today, immobilization is far more common than simple recovery purposes, and immobilization has become an efficient strategy for enzyme feature improvement.…”

Section: Introductionmentioning

confidence: 99%

Encapsulation of lipases by nucleotide/metal ion coordination polymers: enzymatic properties and their applications in glycerolysis and esterification studies

Chen

Song

et al. 2022

J Sci Food Agric

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BACKGROUND In the present study, lipases of TLL (lipase from Thermomyces lanuginosus), AOL (lipase from Aspergillus oryzae), RML (lipase from Rhizomucor miehei), BCL (lipase from Burkholderia cepacia), CALA (Candida antarctica lipase A) and LU (Lecitase® Ultra) were encapsulated into nucleotide‐hybrid metal coordination polymers (CPs). Enzyme concentration was optimized for encapsulation and the enzymatic properties of the obtained lipases were investigated. In addition, their performance in glycerolysis and esterification was evaluated, and glycerolysis conditions (water content, temperature and time) were optimized. RESULTS Hydrolysis activity over 10 000 U g−1 and activity recovery over 90% were observed from AOL@GMP/Tb, TLL@GMP/Tb and RML@GMP/Tb. GMP/Tb encapsulation (of AOL, TLL, RML and LU) improved their thermostability when incubated in air. The encapsulated lipases exhibited moderate [triacylglycerols (TAG) conversion 30–50%] and considerable glycerolysis activity (TAG conversion over 60%). TAG conversions from 69.37% to 82.35% and diacylglycerols (DAG) contents from 58.62% to 64.88% were obtained from CALA@GMP/metal samples (except for CALA@GMP/Cu). Interestingly, none of the encapsulated lipases initiated the esterification reaction. AOL@GMP/Tb, TLL@GMP/Tb, RML@GMP/Tb and CALA@GMP/Tb showed good reusability in glycerolysis, with 88.80%, 94.67%, 89.85% and 78.16% of their initial glycerolysis activity, respectively, remaining after five cycles of reuse. The relationships between temperature and TAG conversion were LnV0 = 6.5364–3.7943/T and LnV0 = 13.8820–6.4684/T for AOL@GMP/Tb and CALA@GMP/Tb, respectively; in addition, their activation energies were 31.55 and 53.78 kJ mol−1, respectively. CONCLUSION Most of the present encapsulated lipases exhibited moderate and considerable glycerolysis activity. In addition, AOL@GMP/Tb, TLL@GMP/Tb, RML@GMP/Tb and CALA@GMP/Tb exhibited good reusability in glycerolysis reactions and potential in practical applications. © 2022 Society of Chemical Industry.

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Section: Introductionmentioning

confidence: 99%

Encapsulation of lipases by nucleotide/metal ion coordination polymers: enzymatic properties and their applications in glycerolysis and esterification studies

Chen

Song

et al. 2022

J Sci Food Agric

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Section: Crosslinked Enzyme Aggregates (Cleas)mentioning

confidence: 98%

“…Covalent bonds formed by enzyme amino groups and aldehyde groups decrease molecular flexibility. This fact suggests positively the increased conformational stability of proteins and, consequently, excellent thermal stability [90,[110][111][112]. The manufacturing process of CLEAs is cost-effective as it does not require the use of preexisting expensive carriers and generally affects heterogeneous biocatalysts with high volumetric activities [113,114].…”

Section: Crosslinked Enzyme Aggregates (Cleas)mentioning

confidence: 99%

Current Status and Future Perspectives of Supports and Protocols for Enzyme Immobilization

Cavalcante

Sousa

et al. 2021

Catalysts

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The market for industrial enzymes has witnessed constant growth, which is currently around 7% a year, projected to reach $10.5 billion in 2024. Lipases are hydrolase enzymes naturally responsible for triglyceride hydrolysis. They are the most expansively used industrial biocatalysts, with wide application in a broad range of industries. However, these biocatalytic processes are usually limited by the low stability of the enzyme, the half-life time, and the processes required to solve these problems are complex and lack application feasibility at the industrial scale. Emerging technologies create new materials for enzyme carriers and sophisticate the well-known immobilization principles to produce more robust, eco-friendlier, and cheaper biocatalysts. Therefore, this review discusses the trending studies and industrial applications of the materials and protocols for lipase immobilization, analyzing their advantages and disadvantages. Finally, it summarizes the current challenges and potential alternatives for lipases at the industrial level.

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“…Covalent bonding is considered one of the strongest chemical interactions between enzymes and supports [86][87][88][89][90][91][92][93][94][95][96]. This immobilization process involves several enzyme residues.…”

Section: Covalent Linkagementioning

confidence: 99%

A Comprehensive Review on the Use of Metal–Organic Frameworks (MOFs) Coupled with Enzymes as Biosensors

et al. 2022

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Several studies have shown the development of electrochemical biosensors based on enzymes immobilized in metal–organic frameworks (MOFs). Although enzymes have unique properties, such as efficiency, selectivity, and environmental sustainability, when immobilized, these properties are improved, presenting significant potential for several biotechnological applications. Using MOFs as matrices for enzyme immobilization has been considered a promising strategy due to their many advantages compared to other supporting materials, such as larger surface areas, higher porosity rates, and better stability. Biosensors are analytical tools that use a bioactive element and a transducer for the detection/quantification of biochemical substances in the most varied applications and areas, in particular, food, agriculture, pharmaceutical, and medical. This review will present novel insights on the construction of biosensors with materials based on MOFs. Herein, we have been highlighted the use of MOF for biosensing for biomedical, food safety, and environmental monitoring areas. Additionally, different methods by which immobilizations are performed in MOFs and their main advantages and disadvantages are presented.

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Chemical and physical Chitosan modification for designing enzymatic industrial biocatalysts: How to choose the best strategy?

Cited by 106 publications

References 778 publications

Encapsulation of lipases by nucleotide/metal ion coordination polymers: enzymatic properties and their applications in glycerolysis and esterification studies

Encapsulation of lipases by nucleotide/metal ion coordination polymers: enzymatic properties and their applications in glycerolysis and esterification studies

Current Status and Future Perspectives of Supports and Protocols for Enzyme Immobilization

A Comprehensive Review on the Use of Metal–Organic Frameworks (MOFs) Coupled with Enzymes as Biosensors

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