Encapsulation of <scp>CALB</scp> by nucleotide/metal ions coordination nanoparticles: highly selective catalysis of esterification while poor performance in glycerolysis reaction

Chen, Wenyi; Xu, Li; Zhong, Nanjing

doi:10.1002/jsfa.11516

Cited by 9 publications

(9 citation statements)

References 61 publications

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“…Encapsulation of lipases into the CPs Lipases of AOL, TLL, RML, CALA, LU and BCL were encapsulated into the GMP/Tb by simple in situ self-assembly of GMP and Tb 3+ . AOL@GMP/Tb was characterized carefully by X-ray diffraction, X-ray photoelectron spectroscopy, Fourier transform infrared spectroscopy, scanning electron microscopy, transmission electron microscopy, confocal laser scanning microscopy and nitrogen-adsorption-desorption, which were presented previously 39 and thus are not shown in the present study.…”

Section: Resultsmentioning

confidence: 99%

“…For CALB, however, nearly totally opposite behavior was observed in our previous study. 39 The encapsulated CALB exhibited quite poor performance in glycerolysis (except for CALB@GMP/Fe), with TAG conversion lower than 5%, despite considerable enzymatic hydrolysis activity. Therefore, the lipase also played a key role in the glycerolysis performance of lipase@CPs.…”

Section: Glycerolysis Of Soybean Oil Catalyzed By Immobilized Lipasesmentioning

confidence: 97%

“…A similar phenomenon was observed for CALB@CPs in our previous study. 39 Therefore, the lipase@GMP/Tb samples were all more suitable in neutral conditions.…”

Section: Stability Of the Immobilized Lipasesmentioning

confidence: 99%

“…However, they exhibited quite poor performance in glycerolysis, with TAG conversion lower than 5%, despite considerable enzymatic hydrolysis activities. 39 Besides the CALB, some other common lipases, including lipase from Thermomyces lanuginosus (TLL), lipase from Aspergillus oryzae (AOL), lipase from Rhizomucor miehei (RML), lipase from Burkholderia cepacia (BCL), Candida antartic lipase A (CALA) and Lecitase® Ultra (LU), are also widely used enzymes. They are commercially available with good properties, in terms of good stability, high actitity, excellent enantioselectivity or broad specificity.…”

Section: Introductionmentioning

confidence: 99%

“…They (most of them) showed good performance in the esterification of fatty acids with glycerol for TAG synthesis. However, they exhibited quite poor performance in glycerolysis, with TAG conversion lower than 5%, despite considerable enzymatic hydrolysis activities 39 …”

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: Resultsmentioning

confidence: 99%

Section: Glycerolysis Of Soybean Oil Catalyzed By Immobilized Lipasesmentioning

confidence: 97%

“…A similar phenomenon was observed for CALB@CPs in our previous study. 39 Therefore, the lipase@GMP/Tb samples were all more suitable in neutral conditions.…”

Section: Stability Of the Immobilized Lipasesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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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Fabrication of immobilized lipases for medium and long‐chain triacylglycerols preparation through solvent‐free acidolysis

Lin,

Zeng,

Zhang

et al. 2024

J Americ Oil Chem Soc

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The present study aims to fabricate efficient immobilized lipases for medium and long‐chain triacylglycerols preparation through acidolysis. Eighteen novel materials, including five mesoporous materials, four organic groups modified SBA‐15 samples (R‐SBA‐15) and nine macroporous resins, were employed as matrices for lipases immobilization. Lipases of TLL, AOL, RML and CALB were evaluated. Results indicated that TLL exhibited better acidolysis performance and decanoic acid content from 30% to 45% could be obtained; while other lipases (CALB, RML, and AOL) showed poor performance. In addition, macroporous resins of DA‐201, ADS‐17, D3520, and mesoporous silicas of SBA‐15, Al‐MCM‐41, HMS, were suitable for TLL immobilization. TLL@SBA‐15 was selected for acidolysis and the reaction conditions were optimized through single factors study and orthogonal design. The optimum conditions for the acidolysis were: lipase amount 6 wt%, decanoic acid: camellia oil molar ratio 14:1, reaction time 12 h and temperature 50°C. Under these conditions, decanoic acid content at 59.87%, oleic acid content 33.99% and sn‐2 decanoic acid content 7.41% was obtained (the mentioned fatty acids here were the fatty acids combined to oil molecules, not free fatty acids).

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Cleaner and sustainable synthesis of high-quality monoglycerides by use of enzyme technologies: techno-economic and environmental study for monolaurin

Mustafa

Fathy

Kutlu

et al. 2023

Clean Techn Environ Policy

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Currently, monoglycerides (MG) are produced using a complicated energy-intensive technology that contributes negatively toward greenhouse gas mitigation. This work suggests a cleaner and simpler one-step enzymatic production of α-monolaurin in an inert membrane reactor, where the reaction and enzyme separation are conducted simultaneously in one unit. Candida antarctica lipase (Lipozyme 435) was used to catalyze the esterification reaction between lauric acid and glycerin in a solvent-free system under mild temperatures. Response surface methodology was used to optimize the reaction conditions. The optimal conditions were a molecular sieve of 14.85% w/w, a temperature of 56.95 °C, an enzyme amount of 5.38% w/w, and a molar ratio of 4.75% w/w. The gas chromatography (GC) analysis showed that the α-monolaurin percentage was 49.5% when the enzymatic process (ENZ) was used. The conventional chemical (CHEM) and autocatalytic (AUT) esterification methods were also performed to study their proportional MG yields. The GC results showed the MG percentages of 43.9 and 41.7% for CHEM and AUT, respectively. Economic analysis was also conducted for the suggested enzymatic technique, and the findings were compared with those of the CHEM and AUT technologies. Using a plant capacity of 4950 t/year and 11% interest for the proposed ENZ process, the total capital investment of α-monolaurin production was preferably four times less than that of the CHEM process and three times less than that of the AUT method, presenting investment possibilities. However, the ENZ process showed the least profitability (net profit per day) among the three processes. Nevertheless, the return on investment and net present value for the ENZ process were preferably higher than those of CHEM and AUT because of its interestingly lower inside battery limit plant cost and less energy consumption. The AUT/CHEM processes generated a total carbon dioxide (CO2) exhaust of 678.7 t CO2 eq./year. In contrast, the ENZ process exhausted a total CO2 of only 50 t CO2 eq./year. The present integrated techno-economic and environmental study of α-monolaurin production emphasizes the green and cost benefits of the proposed ENZ technology. Graphical Abstract

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Encapsulation of CALB by nucleotide/metal ions coordination nanoparticles: highly selective catalysis of esterification while poor performance in glycerolysis reaction

Cited by 9 publications

References 61 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

Fabrication of immobilized lipases for medium and long‐chain triacylglycerols preparation through solvent‐free acidolysis

Cleaner and sustainable synthesis of high-quality monoglycerides by use of enzyme technologies: techno-economic and environmental study for monolaurin

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