Immobilization of Rhizomucor miehei lipase on magnetic multiwalled carbon nanotubes towards the synthesis of structured lipids rich in sn-2 palmitic acid and sn-1,3 oleic acid (OPO) for infant formula use

Ghide, Michael Kidane; Li, Kai; Wang, Jianhua; Abdulmalek, Saadiah A.; Yan, Yunjun

doi:10.1016/j.foodchem.2022.133171

Cited by 27 publications

(5 citation statements)

References 45 publications

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“…However, all immobilized lipase samples exhibited the activity recovery less than 100%. The decreased flexibility of lipase molecules and the lower accessibility of substrates to the lipase-active sites, caused by the interactions between carrier and lipases and the multilayer stacking of lipase molecules, were considered to be the main reasons for the relative low activity recovery . This was further confirmed by the subsequent analysis of the secondary structure (Figure d).…”

Section: Results and Discussionmentioning

confidence: 69%

Enhanced Stability and Performance of Immobilized Lipase Using Hydrophobically Modified Single-Crystalline Ordered Macro–Microporous CuBTC as a Carrier Material

Liu,

Dai,

Liu

et al. 2024

ACS Sustainable Chem. Eng.

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Single-crystalline ordered macro−microporous CuBTC (SOM−CuBTC) is a promising carrier for lipase immobilization due to enhanced mass transfer and stability toward fatty acids. However, the low yield per mass of the template during the preparation process and the water instability of the SOM−CuBTC carrier have posed significant limitations on its practical applications. In this study, we addressed these challenges by introducing a novel dual-solvent system consisting of dimethyl sulfoxide (DMSO) and ethanol to obtain a stable precursor solution with a concentration approximately 10 times higher than that in previous literature, yielding 21.4 mg of SOM−CuBTC per gram of the polystyrene template. However, the decomposition of SOM− CuBTC in an aqueous system of lipase immobilization was observed. We explored chemical vapor deposition and sol−gel methods for hydrophobic modification on SOM−CuBTC. SOM−CuBTC coated by hydrophobic polydimethylsiloxane (PDMS) via the sol− gel method possessed excellent chemical stability and exhibited great potential for lipase immobilization with a significant increase by 98.7% in the specific activity. The obtained immobilized lipase not only showed improved thermal stability and pH tolerance but also displayed excellent catalytic performance in the synthesis process of 1-oleoyl-2-palmitoyl-3-linoleoylglycerol (OPL) by acidolysis. This work reveals the great potential of SOM−CuBTC and provides new insights into the rational design of metal− organic frameworks for enzyme immobilization in extensive applications.

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Section: Results and Discussionmentioning

confidence: 69%

Enhanced Stability and Performance of Immobilized Lipase Using Hydrophobically Modified Single-Crystalline Ordered Macro–Microporous CuBTC as a Carrier Material

Liu,

Dai,

Liu

et al. 2024

ACS Sustainable Chem. Eng.

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“…Given the fact that enzymatic trans-esterification is reversible, the conversion of substrates through this process would be incomplete [ 18 ], and the composition of said substrates could affect their incomplete conversion, indicating that the proper ratio of substrates is of great significance. Thus, the effect of the weight ratio of the MCT to the camellia oil was optimized.…”

Section: Resultsmentioning

confidence: 99%

Enzymatic Synthesis of Structured Lipids Enriched with Medium- and Long-Chain Triacylglycerols via Pickering Emulsion-Assisted Interfacial Catalysis: A Preliminary Exploration

Dong,

Cui,

Jin

et al. 2024

Molecules

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Medium- and long-chain triacylglycerol (MLCT), as a novel functional lipid, is valuable due to its special nutritional properties. Its low content in natural resources and inefficient synthesis during preparation have limited its practical applications. In this study, we developed an effective Pickering emulsion interfacial catalysis system (PE system) for the enzymatic synthesis of MLCT by trans-esterification. Lipase NS 40086 served simultaneously as a catalyst and a solid emulsifier to stabilize the Pickering emulsion. Benefitting from the sufficient oil–water interface, the obtained PE system exhibited outstanding catalytic efficiency, achieving 77.5% of MLCT content within 30 min, 26% higher than that of a water-free system. The Km value (0.259 mM) and activation energy (14.45 kJ mol−1) were 6.8-fold and 1.6-fold lower than those of the water-free system, respectively. The kinetic parameters as well as the molecular dynamics simulation and the tunnel analysis implied that the oil–water interface enhanced the binding between substrate and lipase and thus boosted catalytic efficiency. The conformational changes in the lipase were further explored by FT-IR. This method could give a novel strategy for enhancing lipase activity and the design of efficient catalytic systems to produce added-value lipids. This work will open a new methodology for the enzymatic synthesis of structured lipids.

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“…Interestingly, Ghide et al (2022) have used Rhizomucor miehei lipase immobilized on magnetic multi‐walled carbon the synthesis of 1,3‐dioleoyl‐2‐palmotoylglycerol (OPO)‐rich human milk fat substitutes nanotubes suggest that the immobilized fungal lipase is a promising biocatalyst for the synthesis of OPO‐rich triacylglycerols with potential use in infant formulas.…”

Section: Biotechnological Applicationsmentioning

confidence: 99%

Fungal lipases as biocatalysts: A promising platform in several industrial biotechnology applications

Mahfoudhi

Benmabrouk

Fendri

et al. 2022

Biotech & Bioengineering

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Many researchers have found fungi as a reliable source of lipase due to the versatility of their properties, ease of mass production, thermal stability, pH stability, broad substrate specificity, retained activity in organic solvents, and their low‐cost extraction procedure. This review paper presents an overview about the main aspects of fungal lipases screened from several types of strains as well as their use as biocatalysts. Additionally, some biochemical properties will be reported. As commonly known, lipases can be produced from animals, plants, and microorganisms. Compared to other lipases, those obtained from fungi have been found to be more productive, a fact that encouraged the massive production of most fungal lipases due to their considerable commercial importance during the past few years. This paper is concerned about some of the major characteristics that made fungal lipases desirable products in the industrial fields. Due to the enantioselective properties of fungal lipases and their ability to remain active under extreme temperature, pH, and organic solvents, enzymes are capable to synthesize esters as well as to catalyze a variety of chemical reactions that include esterification, transesterification, acidolysis and aminolysis in aqueous and nonaqueous media. Furthermore, lipases are considered to have a commercial importance for biotechnological application fields, which makes them increasingly popular in food, detergent, cosmetic, organic synthesis, and pharmaceutical domains. The biotechnological potential of lipases has made the latter a coveted choice in industries for the present and future as biocatalysts. In addition, a classification of these fungal enzymes is also highlighted in this review. Moreover, the impact of an immobilization strategy of these fungal strains to achieve higher yields and to improve their production is discussed. Finally, fungal enzymes have played a crucial role from ancient times to today in different fields using several types of biological systems, which gives them a great interest for the production of these enzymes in large amounts with low cost and easy viability to enlarge their use in many industries. Likewise, some future perspectives on lipase production will also be discussed by focusing on special cases on lipase engineering.

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Immobilization of Rhizomucor miehei lipase on magnetic multiwalled carbon nanotubes towards the synthesis of structured lipids rich in sn-2 palmitic acid and sn-1,3 oleic acid (OPO) for infant formula use

Cited by 27 publications

References 45 publications

Enhanced Stability and Performance of Immobilized Lipase Using Hydrophobically Modified Single-Crystalline Ordered Macro–Microporous CuBTC as a Carrier Material

Enhanced Stability and Performance of Immobilized Lipase Using Hydrophobically Modified Single-Crystalline Ordered Macro–Microporous CuBTC as a Carrier Material

Enzymatic Synthesis of Structured Lipids Enriched with Medium- and Long-Chain Triacylglycerols via Pickering Emulsion-Assisted Interfacial Catalysis: A Preliminary Exploration

Fungal lipases as biocatalysts: A promising platform in several industrial biotechnology applications

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