Biosynthesis of benzyl cinnamate using an efficient immobilized lipase entrapped in nano-molecular cages

Cao, Yiping; Zhi, Gao‐Ying; Han, Li; Chen, Queting; Zhang, Dong‐Hao

doi:10.1016/j.foodchem.2021.130428

Cited by 25 publications

(6 citation statements)

References 39 publications

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“…The primary amino group content on PEI@PVAC magnetic microspheres is detected via the p-nitrobenzaldehyde colorimetry method. 15 Preparation of SH-PEI@PVAC Microspheres and Detection of the Thiol Group. SH-PEI@PVAC magnetic microspheres are obtained by modifying the thiol group on PEI@PVAC magnetic microspheres using 3-mercaptopropionic acid (MPA).…”

Section: Discussionmentioning

confidence: 99%

“…The adsorption amount of lipase is determined by detecting lipase concentrations in the supernatant using the Bradford method. 15 In the experiment of desorption, 25 mg of the adsorbed lipase or the encapsulated lipase is added into 2 mL of NaCl water solution (1.5 or 3 M) with N 2 protection. After culturing at 160 r/min at 25 °C for 4 h, the immobilized lipase is collected.…”

Section: Discussionmentioning

confidence: 99%

“…After reaction, PEI@ PVAC magnetic microspheres are collected and dried. The primary amino group content on PEI@PVAC magnetic microspheres is detected via the p -nitrobenzaldehyde colorimetry method …”

Section: Methodsmentioning

confidence: 99%

“…(a) Chemical structure of PEI and PEGDGE, as well as the scheme of lipase encapsulated in nanomolecular cages on the magnetic microsphere surface. Figure was reproduced from ref with permission from copyright holders; (b) optical microscope and (c) SEM image of PVAC magnetic microspheres; (d) particle size distribution of PVAC magnetic microspheres; (e) magnetic responsiveness and redispersibility of PVAC magnetic microspheres.…”

Section: Introductionmentioning

confidence: 99%

“…14 Recently, our group established a kind of birdcage-like structure named nanomolecular cage on the support surface by grafting polyethyleneimine (PEI), modifying N-succinimidyl-3-(2-pyridyldithiol) propionate (SPDP) on PEI, and subsequently crosslinking PEI and used these nanomolecular cages to encapsulate lipase. 15 By encapsulating lipase in cages on the surface of microspheres, lipase could not only retain the active conformation but also bind firmly to the support, which combined the advantage of physical adsorption with minimal damage on enzyme activity and the advantage of covalent binding with firm immobilization. As a result, lipase encapsulated in the cages showed good activity and high stability.…”

Section: ■ Introductionmentioning

confidence: 99%

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Improving the Encapsulation Efficiency of Lipase in Molecular Cages and Its Application

et al. 2023

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Here, lipase encapsulation is constructed by locking enzyme molecules in nanomolecular cages on the surface of SH-PEI@PVAC magnetic microspheres. To improve the encapsulation efficiency in enzyme loading, the thiol group is efficiently modified on the grafted polyethyleneimine (PEI) using 3-mercaptopropionic acid. N2 adsorption–desorption isotherms reveal the existence of mesoporous molecular cages on the microsphere surface. The robust immobilizing strength of carriers to lipase demonstrates the successful encapsulation of enzymes in nanomolecular cages. The encapsulated lipase shows high enzyme loading (52.9 mg/g) and high activity (51.4 U/mg). Different sizes of molecular cages are established, and the cage size showed important effects on lipase encapsulation. It shows that enzyme loading is low at a small size of molecular cages, which is attributed to that the nanomolecular cage is too small to house lipase. The investigation in lipase conformation suggests that the encapsulated lipase retains its active conformation. Compared with the adsorbed lipase, the encapsulated lipase shows higher thermal stability (4.9 times) and higher resistance to denaturants (5.0 times). Encouragingly, the encapsulated lipase shows high activity and reusability in lipase-catalyzed synthesis of propyl laurate, suggesting the potential application value of encapsulated lipase.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: ■ Introductionmentioning

confidence: 99%

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Improving the Encapsulation Efficiency of Lipase in Molecular Cages and Its Application

et al. 2023

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Synthesis of isobutyl cinnamate based on DESs catalyst: Optimization and kinetics

Xu,

Zhao,

Zeng

et al. 2024

Int J of Chemical Kinetics

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In this work, the optimum process conditions and kinetics of the green synthesis of isobutyl cinnamate using deep eutectic solvents (DESs) as catalysts were investigated. Isobutyl cinnamate is a spice with low toxicity and is widely used in the food industry. However, there is a lack of reports on its green synthesis. Three DESs were prepared by adjusting the mixing ratio of choline chloride (ChCl) and p‐toluenesulfonic acid (PTSA). Response surface methodology with Box‐Behnken design (RSM‐BBD) was used to optimize the process parameters of the esterification of cinnamic acid with isobutanol. The effects of catalyst loading, stirring speed, cinnamic acid/isobutanol molar ratio, and temperature on the conversion of cinnamic acid over time were evaluated. Using ChCl‐PTSA as a catalyst, the kinetics data and chemical equilibrium constants of the esterification were determined at a temperature range of 353.15–383.15 K. The pseudo‐homogeneous (PH) model based on activity was then adopted to describe the kinetics of the reaction, and the relative deviations between the experimental values and the calculated ones by PH model are less than 5.5%. Thermodynamic data (ΔrH0, ΔrS0, ΔrG0) for the esterification reaction was calculated as well. In addition, the results of six consecutive cycles of the catalyst showed that ChCl‐PTSA has good stability and recyclability.

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Improved catalytic performance of carrier-free immobilized lipase by advanced cross-linked enzyme aggregates technology

Xia

Yan

Zou

et al. 2021

Bioprocess Biosyst Eng

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The cross-linked enzyme aggregates (CLEAs) are one of the technologies that quickly immobilize the enzyme without a carrier. This carrier-free immobilization method has the advantages of simple operation, high reusability and low cost. In this study, ionic liquid with amino group (1-aminopropyl-3methylimidazole bromide IL) was used as the novel functional surface molecule to modify industrialized lipase (Candida rugosa lipase, CRL). The enzymatic properties of the prepared CRL-FIL-CLEAs were investigated. The activity of CRL-FIL-CLEAs (5.51 U/mg protein) was 1.9 times higher than that of CRL-CLEAs without surface modi cation (2.86 U/mg protein). After incubation at 60℃ for 50 min, CRL-FIL-CLEAs still maintained 61% of its initial activity, while the value for CRL-CLEAs was only 22%. After repeated use for ve times, compared with the 22% residual activity of CRL-CLEAs, the value of CRL-FIL-CLEAs was 51%. Further kinetic analysis indicated that the Km values for CRL-FIL-CLEAs and CRL-CLEAs were 4.80 mM and 8.06 mM, respectively, which was inferred that the a nity to substrate was increased after modi cation. Based on the above results, it was indicated that this method provided a new idea for the effective synthesis of immobilized enzyme. HighlightsNovel immobilized lipase was prepared with carrier-free immobilization method.The aggregates of ionic liquid and lipase proved to be an e cient catalyst.The activity and stability of carrier-free immobilized lipase were improved.The activity of the novel aggregates reached 1.9 times of conventional lipase.

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Biosynthesis of benzyl cinnamate using an efficient immobilized lipase entrapped in nano-molecular cages

Cited by 25 publications

References 39 publications

Improving the Encapsulation Efficiency of Lipase in Molecular Cages and Its Application

Improving the Encapsulation Efficiency of Lipase in Molecular Cages and Its Application

Synthesis of isobutyl cinnamate based on DESs catalyst: Optimization and kinetics

Improved catalytic performance of carrier-free immobilized lipase by advanced cross-linked enzyme aggregates technology

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