Lipases Immobilized onto Nanomaterials as Biocatalysts in Biodiesel Production: Scientific Context, Challenges, and Opportunities

Oliveira, André Luiz Barros de; Cavalcante, Francisco Sales Ávila; Moreira, Katerine S.; Monteiro, Rodolpho R. C.; Rocha, Thales Guimarães; Souza, José E. S.; Fonseca, Aluísio Marques da; Lopes, Ada Amélia Sanders; Guimarães, Artemis Pessoa; Lima, Rita Karolinny Chaves de; Souza, Monique

doi:10.21577/1984-6835.20210019

Cited by 37 publications

(21 citation statements)

References 170 publications

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“…In the encapsulation protocol, no physical interactions or chemical bonds are established between the enzyme and the support, and it therefore maintains the stability. 21 On the other hand, free enzyme may experience protein aggregation (mainly near to the isoelectric point). This may be caused by undesired enzyme interactions where inactivation that can stabilize incorrect enzyme structures.…”

Section: Stability Of the Immobilized Lipasesmentioning

confidence: 99%

“…20 However, the substrate may have difficulty accessing the enzyme's active site, and the inhibitory effects by products or substrates within the porous matrix are possible. 21 The mechanisms involved in the reactions with protein structures are highly complex because of the strong influence of some parameters such as chemical concentration, average pH, density of groups in the materials, and reaction time with respect to its reactivity and chemical structure. 2,22 Nevertheless, enzymatic properties of the immobilized lipases could be modulated by altering the immobilization conditions.…”

Section: Introductionmentioning

confidence: 99%

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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: Stability Of the Immobilized Lipasesmentioning

confidence: 99%

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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“…Low concentrations of glutaraldehyde make the enzyme fixation process easier [104][105][106]. In contrast, a higher glutaraldehyde concentration enables many aldehyde groups that interact with the enzyme, making the enzyme immobilization process more efficient and preventing leaching [107][108][109]. The presence of glutaraldehyde as a functional binding agent contributes to high stability in immobilized enzymes.…”

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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“…Additionally, immobilized enzymes show very little to no allergenicity, high recoveries, and a reuse capacity, rendering processes more economical [ 29 , 53 ]. To increase the stability of the enzymes during storage and make them more resistant to operational conditions, several types of support for enzyme immobilization have been studied, including magnetic nanoparticles, sol-gels, mesoporous silica, and polymers [ 17 , 27 , 43 , 54 , 55 , 56 , 57 , 58 , 59 , 60 , 61 , 62 , 63 , 64 , 65 , 66 , 67 , 68 , 69 , 70 , 71 , 72 . Immobilization technologies can also prevent subunit dissociation, aggregation, autolysis, and proteolysis, apart from delivering more suitable reaction microenvironments [ 73 , 74 , 75 , 76 ].…”

Section: Introductionmentioning

confidence: 99%

The Chemistry and Applications of Metal–Organic Frameworks (MOFs) as Industrial Enzyme Immobilization Systems

et al. 2022

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Enzymatic biocatalysis is a sustainable technology. Enzymes are versatile and highly efficient biocatalysts, and have been widely employed due to their biodegradable nature. However, because the three-dimensional structure of these enzymes is predominantly maintained by weaker non-covalent interactions, external conditions, such as temperature and pH variations, as well as the presence of chemical compounds, can modify or even neutralize their biological activity. The enablement of this category of processes is the result of the several advances in the areas of molecular biology and biotechnology achieved over the past two decades. In this scenario, metal–organic frameworks (MOFs) are highlighted as efficient supports for enzyme immobilization. They can be used to ‘house’ a specific enzyme, providing it with protection from environmental influences. This review discusses MOFs as structures; emphasizes their synthesis strategies, properties, and applications; explores the existing methods of using immobilization processes of various enzymes; and lists their possible chemical modifications and combinations with other compounds to formulate the ideal supports for a given application.

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Lipases Immobilized onto Nanomaterials as Biocatalysts in Biodiesel Production: Scientific Context, Challenges, and Opportunities

Cited by 37 publications

References 170 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

The Chemistry and Applications of Metal–Organic Frameworks (MOFs) as Industrial Enzyme Immobilization Systems

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