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CATALYSIS COMMUNICATIONS · 2013 · IF 2.915

Biocatalytic synthesis of short-chain flavor esters with high substrate loading by a whole-cell lipase from Aspergillus oryzae

Hong-De Yan,Qun Zhang,Zhao Wang

A lipase from Aspergillus oryzae WZ007 exhibited high esterification activities toward a series of short-chain acids and alcohols. Moreover, it displayed a strong tolerance for high substrate concentration of up to 2.0   M and presented a highest initial rate of 276   mmol·L −   1 ·h −   1 at this concentration. After a reaction time of 48   h, the conversion rates of acids were higher than 80% for the synthesis of a majority of heptanoic acid esters, some octanoic acid esters and n -propyl hexanoate. These results implied that A. oryzae WZ007 lipase was a promising biocatalyst in the production of flavor esters.

研究领域: 生物化学 · 食品科学
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LWT-FOOD SCIENCE AND TECHNOLOGY · 2024 · IF 6

Insights into the enzymatic synthesis of alcoholic flavor esters with molecular docking analysis

Yiran Bian,Yi Zhang,Taosuo Wang,Chuang Yang,Zhiming Feng,Kheng-Lim Goh,Yibin Zhou,Mingming Zheng

The enzymatic synthesis is essential for the flavor esters in the food and fragrance industries. This paper introduces a novel preparation method for lipase microarrays (CALB@PMHOS-TEOS) with loadings up to 229 ± 1.4 mg/g. Using surfactant-free hydrophobic silica-hybridized mesoporous materials and Candida antarctica lipase, this resulted in the effective synthesis of flavor esters. Using CALB@PMHOS-TEOS a Pickering emulsion system was formed at the oil-water interface for the sustainable synthesis of flavor esters. This resulted in a 93.5 ± 0.5 % conversion of hexanoic acid within 2 h at an optimal temperature of 35 °C, which is the highest level recorded in the literature to date. Furthermore, the conversion of hexanoic acid was maintained at 63.9 ± 1.2 % after 9 cycles of CALB@PMHOS-TEOS reuse. The application of the enzyme to the synthesis in a variety of flavor esters achieved a new benchmark in the existing literature. A molecular docking model was evaluated to understand the molecular mechanism underpinning the immobilized lipase. This work introduces a novel method for the eco-friendly and efficient synthesis of flavor esters for applications across various fields including food and cosmetics.

研究领域: 食品科学 · 生物化学 · 材料科学
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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES · 2025 · IF 8.5

Immobilized lipase on MIL-53(Al)-AM11 with regulatable hydrophobic surface for flavor ester synthesis

Le Zhong,Yuxiao Feng,Zichen Wang,Tian Tian,Yali Bi,Jiandong Cui

Enzymatic synthesis of flavor esters is crucial for applications in food, beverage, and cosmetics industries. However, the poor activity and stability of free lipase hinder these reaction. Inspired by the concept of lipase interface activation, MIL-53(Al)-NH 2 was modified with alkyl acid anhydrides of varying chain lengths to tailor its hydrophobicity, and Candida Rugosa lipase (CRL) was subsequently immobilized on this surface to achieve efficient interface activation. The resulting CRL@MIL-53(Al)-AM11 exhibited 3.5 times higher activity than the unmodified CRL@MIL-53(Al)-NH 2 . Moreover, CRL@MIL-53(Al)-AM11 enabled one-step purification of crude CRL via selective adsorption. It also showed enhanced storage and thermal stability as well as higher resistance to protease degradation and denaturants than free CRL. CRL@MIL-53(Al)-AM11 retained 75 % of its initial activity after 30 min treatment at 55 °C, whereas the free CRL retained only 41 %. After 11 days of storage, CRL@MIL-53(Al)-AM11 maintained 70 % of its initial activity, in contrast to 36 % for the free lipase. Notably, CRL@MIL-53(Al)-AM11 achieved a 97 % conversion rate in the esterification synthesis of the flavoring substance (butyl butyrate) within 24 h and retained over 40 % conversion after five consecutive cycles. Therefore, this strategy offers a feasible approach for constructing high-performance immobilized lipases for flavor ester synthesis.

CAS / MDL: 109-21-7
研究领域: 生物化学 · 食品科学 · 酶工程
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Frontiers of Chemical Science and Engineering · 2020 ·Vol. 14 ·期 5 ·868-879 · IF 3.552

Expression and characterization of a CALB-type lipase from Sporisorium reilianum SRZ2 and its potential in short-chain flavor ester synthesis

Shen Jiang-Wei,Cai Xue,Dou Bao-Juan,Qi Feng-Yu,Zhang Xiao-Jian,Liu Zhi-Qiang,Zheng Yu-Guo

A lipase from Sporisorium reilianum SRZ2 (SRL) with 73% amino acid sequence identity to Candida antarctica lipase B (CALB) was cloned and overexpressed in Pichia pastoris . The recombinant SRL showed a preference for short-chain p -nitrophenyl esters. It achieved maximum activity at pH 8.0 and 65°C for p -nitrophenyl hexanoate (C6) with K m and k cat / K m values of 0.14 mmol·L −1 and 1712 min −1 · mmol · L −1 at 30°C, respectively. SRL displayed excellent thermostability and pH stability, retaining more than 79% of its initial activity after incubation at 60°C for 72 h and 75% at pH 3 to 11 for 72 h. It also maintained most of its activity in the presence of inhibitors and detergents except sodium dodecyl sulfate, and it tolerated organic solvents. SRL was covalently immobilized and successfully used for ethyl hexanoate synthesis in cyclohexane or in a solvent-free system with a high conversion yield (> 95%). Furthermore, high conversion yield was also achieved for the synthesis of various short-chain flavor esters when high substrate concentrations of 2 mol · L −1 were applied. This study indicated that a CALB-type lipase from S. reilianum SRZ2 showed great potential in organic ester synthesis.

CAS / MDL: 100-02-7
研究领域: 生物化学 · 酶工程 · 食品科学
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LWT-FOOD SCIENCE AND TECHNOLOGY · 2022 · IF 6.056

Efficient and sustainable preparation of cinnamic acid flavor esters by immobilized lipase microarray

Jinhang Chen,Yi Zhang,Huaying Zhong,Hao Zhu,Hongxun Wang,Kheng-Lim Goh,Juntao Zhang,Mingming Zheng

Green and effective synthesis of flavor esters is a long-term interest in food, cosmetic and pharmaceutical industries. Here, an immobilized lipase microarray was prepared by immobilizing lipase CSL on hydrophobically modified ordered mesoporous silicon (CSL@OMS-C 8 ) for the enzymatic production of cinnamic esters with different flavors. The results showed that the CSL@OMS-C 8 , with an immobilization capacity of 249.3 ± 11.1 mg/g, exhibited 1.6 times higher catalytic activity than that of free lipase at the optimum temperature of 70 °C. The maximum yield of benzyl cinnamate reached 97.3% in 2 h with the corresponding CE value of 650.5 μmol/g · h, leading to the highest record compared to the current literature. Besides, the CSL@OMS-C 8 could maintain 81.4 ± 1.1% conversion for cinnamic acid after five-cycle reuse, thus revealing the high stability and reusability of immobilized lipase. Finally, the broad applicability of the immobilized lipase microarray was confirmed by its capacity to successfully catalyze the synthesis of methyl cinnamate, ethyl cinnamate, butyl cinnamate, geranyl cinnamate and isoamyl cinnamate. This study reveals new insights on the efficient and sustainable enzymatic approach to produce natural cinnamic acid flavor esters and, consequently, could pave the way for the natural and clean production in food industries.

研究领域: 食品科学 · 生物催化 · 绿色化学
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JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY · 2025 · IF 6.2

Novel Immobilized Enzyme System Using Hydrophobic Dendritic Mesoporous Silica Nanospheres for Efficient Flavor Ester Production

Run Liu,Qi Zhou,Yi Zhang,Yuanzhi Xu,Zhonghui Liu,Kheng-Lim Goh,Vladimir Zivkovic,Mingming Zheng

Enzymatic synthesis of flavor esters is widely used in the food and flavor industries, but challenges remain in improving the catalytic efficiency and stability of biocatalysts. This study evaluates the performance of a novel biocatalyst, CALB@DMSN-C8, formed by immobilizing Candida antarctica lipase B (CALB) on hydrophobic dendritic mesoporous silica nanospheres (DMSN-C8), for synthesizing flavor esters. The CALB@DMSN-C8 catalyst achieves a caproic acid conversion rate of 98.5 ± 0.5% in just 30 min and demonstrates outstanding thermal stability, retaining a high conversion efficiency over 20 reuse cycles. To our knowledge, this study represents the most efficient synthesis of flavor esters, including ethyl valerate, ethyl caproate, ethyl heptanoate, and ethyl caprylate, compared to studies in the existing literature. Analysis of aroma characteristics and molecular docking simulations revealed the typical flavor profiles and synthesis mechanisms of various mellow esters. This study develops an innovative strategy by using self-made immobilized lipases to catalyze the production of flavor esters with potential applications in food and cosmetics.

研究领域: 食品科学 · 酶工程 · 生物催化
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ACS Sustainable Chemistry & Engineering · 2023 · IF 8.4

Ultraviolet/Visible Light-Responsive Pickering Interfacial Biocatalysis: Efficient and Robust Platform for Bioconversions

Huaying Zhong,Yi Zhang,Yangmin Gong,Chuyun Wan,Yufei Zhang,Mingming Zheng

Stimuli-responsive Pickering interfacial biocatalysis (PIB) platforms are highly desirable due to their convenient product extraction and catalyst recovery. Light-responsive PIB stabilized by immobilized biocatalyst particles, which serve as both emulsifiers and catalysts, have not attracted enough attention. Herein, a novel and effective ultraviolet/visible light-responsive PIB system is proposed to facilitate reversible emulsification/demulsification. The modified hollow mesoporous silica nanospheres (HMSS-N) with photochromic spiropyran (SP-COOH) were utilized as a light-responsive emulsifier and carrier of lipase CL (CL@HMSS-SP). The light-responsive performance and catalytic performance of the PIB system were also studied in detail. As a result, the O/W emulsion demulsification or emulsification could be easily accomplished by inducing ultraviolet or visible light to change the surface wettability of the smart emulsifiers. The system exhibited the highest catalytic activity in the model esterification reaction between n-hexanol acid and 1-hexanol that has been reported so far (a catalytic efficiency value of 80.9 mmol g–1 h–1), which is a 12.6-fold enhancement compared with the conventional free enzyme one-phase system. The robust system maintained high catalytic activity even after 10 cycles, averaging 148.2 g of product g–1 biocatalyst. Thus, the ultraviolet/visible light-responsive PIB gives insights into the biocatalytic synthesis of flavor esters with high efficiency and stable reusability and shows great potential for cleaner production in the future.

研究领域: 化学工程 · 生物技术 · 材料科学 · 催化
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FOOD CHEMISTRY · 2024 · IF 8.5

Ultrasound-assisted enzymatic synthesis of cinnamyl acetate by immobilized lipase on ordered mesoporous silicon with CFD simulation and molecular docking analysis

Jinhang Chen,Tieliang Liu,Yi Zhang,Lu Zheng,Kheng-Lim Goh,Vladimir Zivkovic,Mingming Zheng

Flavor esters are used in food and cosmetic industries, but sustainable production remains a big challenging. This study proposed the ultrasound-assisted biosynthesis of cinnamyl acetate using self-made immobilized lipase CSL@OMS-C 8 , with computational fluid dynamics (CFD) and molecular simulations revealing the hydrodynamic properties and lipase-catalytic mechanisms. The results demonstrate that ultrasonication-intensified enzymatic reaction facilitated 96.6 % conversion of cinnamic alcohol, due to the ultrasound-assisted catalytic efficiency of 13.7 mmol/g·min. Molecular docking analysis identifies the lowest binding energy of −3.7 kcal·mol −1 between lipase and vinyl acetate, contributing to the highest conversion rates compared to acetic acid, ethyl acetate. CFD simulation indicates that ultrasonic energy waves promote substrate diffusion and mixing with lower shear stress. The catalytic stability of CSL@OMS-C 8 was confirmed by 60.1 % of relative activity after 10-time reuse. This paper theoretically and experimentally studied the ultrasonic-assisted enzymatic synthesis of cinnamyl acetate, showcasing huge potential for sustainable production of flavor esters.

研究领域: 生物技术 · 化学工程 · 食品科学 · 材料科学 · 计算化学
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