LWT-FOOD SCIENCE AND TECHNOLOGY
·
2020
·
IF 4.006
Yan-yan Huang,Jia-jia Yu,Qin-yu Zhou,Li-na Sun,Dong-mei Liu,Ming-hua Liang
Yogurt-flavored bases are widely used in food industry for enhancing flavors. In this study, yogurt-flavored bases by mixed lactic acid bacteria with or without lipase were investigated, which included Streptococcus lactis ACCC 11093 (SL) and Lactobacillus casei subsp. rhamnosus 6013 (LCR), SL and Lactobacillus acidophilus 1.1878 (LAP), and SL and Lactobacillus plantarum DMDL 9010 (LP), respectively. Compared with the combination of SL and LCR and the combination of SL and LAP, the combination of SL and LP had higher production of total amino acids , volatile acids and esters, suggesting that the combination of SL and LP was more efficient to produce yogurt-flavored bases. In addition, lipase significantly increased the production of amino acids associated with sweet and bitter flavors, and resulted in rougher milk globule surface and tighter network structure compared with fermentations without the addition of lipase. Furthermore, a total of 54 volatile compounds were detected in yogurt-flavored bases. The production of volatile compounds in fermentations with and without the addition of lipase, was mainly affected by acids and esters, respectively. Therefore, the lipase is a favorable supplement for producing yogurt-flavored bases.
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PROTEIN EXPRESSION AND PURIFICATION
·
2018
·
IF 1.338
Jian-yong Zheng,Xing Lan,Xiao-jun Li,Li-juan Huang,Yin-jun Zhang,Zhao Wang
Pichia pastoris expression is a mature and efficient eukaryotic expression system . In this work, Aspergillus oryzae lipase (AOL, with the molecular mass of 28 kDa), which can perform highly stereoselective hydrolysis of (R, S)-methyl 2-(4-hydroxyphenoxy) propanoate, was expressed in P . pastoris X-33. The specific activity of AOL was 432 U/mg, which was obtained by fed-batch cultivation in a 5 L bioreactor using a methanol feeding strategy. After fermentation, the supernatant was concentrated by ultrafiltration with a 10 kDa cut-off membrane and purified with DEAE-Sepharose™ FF ion-exchange chromatography and phenyl Seflnose™ 6 FF hydrophobic interaction chromatography . The purified lipase activity reached 5509 U/mg. AOL showed high activity toward short-chain triacylglyceride (C 4 ), and the optimum temperature and pH were 40 °C and 8.0, respectively. The purified enzyme activity was inhibited by Zn 2+ and Cu 2+ . Moreover, the K m and V max values were 1 mM and 32.89 mmol/min, respectively.
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RENEWABLE ENERGY
·
2021
·
IF 8.001
Le Zhong,Xiaobo Jiao,Hongtong Hu,Xuejian Shen,Juan Zhao,Yuxiao Feng,Conghai Li,Yingjie Du,Jiandong Cui,Shiru Jia
In this study, the surfactant activated lipase from Aspergillus oryzae was used to prepare magnetic hybrid nanoflowers by embedding Fe 3 O 4 magnetic nanoparticles (MNPs) into hybrid nanoflowers (MhNF). Meanwhile, MNPs were integrated into the activated lipase hybrid nanoflowers through covalent cross-linking (cross-linked-MhNF). Activity recovery of the MhNF and cross-linked-MhNF was 190% and 174%, respectively. However, activity recovery of lipase hybrid nanoflowers (hNF) only retained 77%. Furthermore, the MhNF displayed higher K cat /K m value than free lipase, indicating high catalytic efficiency of MhNF. Compared with free lipase, the MhNF exhibited high tolerance against methanol and storage stability. Furthermore, the MhNF could be easily recycled by magnet without obvious activity loss. After reusing for 10 cycles, the activated hNF only retained 26% activity of its original activity, while the MhNF still maintained 84% activity of its initial activity, indicating excellent reusability . In the reaction of producing biodiesel from soybean oil, the MhNF-catalyzed biodiesel yield reached 88%, while the free enzyme was only 69%. The yield of biodiesel catalyzed by MhNF was maintained at 76% even after 6 consecutive cycles.
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Catalysts
·
2019
·Vol. 9
·期 11
·914
·
IF 3.444
Huixia Yang,Weiwei Zhang
Enzymatic production of biodiesel from waste cooking oil (WCO) could contribute to resolving the problems of energy demand and environment pollutions.In the present work,Burkholderia cepacialipase (BCL) was activated by surfactant imprinting, and subsequently immobilized in magnetic cross-linked enzyme aggregates (mCLEAs) with hydroxyapatite coated magnetic nanoparticles (HAP-coated MNPs). The maximum hyperactivation of BCL mCLEAs was observed in the pretreatment of BCL with 0.1 mM Triton X-100. The optimized Triton-activated BCL mCLEAs was used as a highly active and robust biocatalyst for biodiesel production from WCO, exhibiting significant increase in biodiesel yield and tolerance to methanol. The results indicated that surfactant imprinting integrating mCLEAs could fix BCL in their active (open) form, experiencing a boost in activity and allowing biodiesel production performed in solvent without further addition of water. A maximal biodiesel yield of 98% was achieved under optimized conditions with molar ratio of methanol-to-WCO 7:1 in one-time addition in hexane at 40 °C. Therefore, the present study displays a versatile method for lipase immobilization and shows great practical latency in renewable biodiesel production.Keywords:biodiesel;waste cooking oil;lipase immobilization;interfacial activation;functionalized magnetic nanoparticles
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Food Bioscience
·
2020
·
IF 3.067
Liang Gao,Xinyi Cheng,Xuwei Yu,Xiaosan Wang,Qingzhe Jin,Xingguo Wang
1-Oleoyl-2-palmitoyl-3-linoleoylglycerol (OPL) is a critical structured lipid in human milk fat and it plays an important role in infants' health. The development of an efficient method for such compound preparation is necessary. In this study, one- and two-step methods for OPL production by enzymatic acidolysis of fractionated palm stearin with mixed acids were compared in solvent-free and solvent systems. The results demonstrated that in the solvent system, the OPL contents by the one- and two-step methods were 45.8% and 56.7%, respectively. In the solvent-free system, the one- and two-step methods resulted in the formation of 43.7% and 54.8% OPL, respectively. Subsequently, acidolysis conditions of the two-step method were optimized. Under the optimum conditions, the content of OPL was 57.7%, and 83.2% of palmitic acid was at the sn-2 position . The prepared OPL has potential to be applied in infant formulas.
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NEW JOURNAL OF CHEMISTRY
·
2023
·Vol. 47
·期 44
·20316-20321
·
IF 3.3
Yong Tang,Kaifu Zhang,Yuelin Xu,Jinglin Ma,Hanqing Xie,Hongquan Zhang,Yanmin Jiang,Rui Zhao,Lei Wang
A green and efficient method for the construction of functionalized 2,3-dihydrothiophene derivatives in water was reported. In this work, Novozym 435 acted as a remarkable biocatalyst in catalyzing the four-component reaction of aldehydes, malonitrile or ethyl cyanoacetate, 1,3-thiazolidinedione, and amines under mild conditions. Excellent yields (85–95%) of all the corresponding products could be obtained in reasonable reaction time. Moreover, Novozym 435 could be reused for six cycles with a yield of at least 80%. The rationality of this multicomponent reaction mechanism was also verified via control experiments.
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JOURNAL OF CHEMICAL TECHNOLOGY AND BIOTECHNOLOGY
·
2016
·Vol. 92
·期 6
·1203-1210
·
IF 2.738
Fengli Wang,Guanglei Zhao,Xiongfei Lang,Junrong Li,Xiaofeng Li
BACKGROUND Long-chain cellulose esters can be used as packaging materials, film materials, biodegradable plastics and drug delivery agents. Chemical methods are commonly adopted for preparation of these esters using traditional chemical catalysts and organic solvents, which result in environmental and safety problems. RESULT A new enzymatic method was tested for synthesis of long-chain cellulose esters in mixed ionic liquids. The key reaction conditions, including mass ratio of ionic liquids, acylating agents, lipase/cellulose mass ratio, reaction temperature and substrate molar ratio, showed significant influences on enzymatic acylation. FT-IR and 1 H NMR spectra indicated the successful acylation of hydroxyl groups. SEM and XRD data showed significant changes in morphologies and crystallinity. The thermal properties of products were different from the original due to the disruption effect of ILs and the enzymatic acylation. CONCLUSION A facile one-step route is presented for synthesis of long-chain cellulose esters. The lipase-catalyzed synthesis is an ecofriendly and green approach for the modification of cellulose by replacing traditional chemical catalysts with enzymes and replacing organic solvents with ionic liquids. This biocatalytic approach may find its applications in preparation of potentially biodegradable materials for food, pharmaceutical and related industries. © 2016 Society of Chemical Industry
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Molecular Catalysis
·
2022
·
IF 5.089
Bin Zou,Feng Liu,Yan Yan,Ting Feng,Josephine Naa Norkor Dowuona
In this study, coupling with substrate ultrasonic pretreatment technology, magnetic cross-linked enzyme aggregates (CRL-FIL-CLEAs@Fe 3 O 4 ) was used as novel biocatalyst for efficient preparation of phytosterol oleate in solvent-free reaction system. The CRL loading was 0.16 mg protein/mg CRL-FIL- CLEAs@Fe 3 O 4 . The effects of ultrasonic parameters, catalyst dosage, substrate molar ratio, and reaction temperature on the synthesis of phytosterol esters were studied. The results showed that the catalytical properties of CRL-FIL-CLEAs@Fe 3 O 4 (7.09±0.11 µmol phytosterol/mg protein. hour) was significantly improved compared with natural lipase from Candida rugosa (CRL, 5.13±0.21 µmol phytosterol/mg protein. hour). Simultaneously, ultrasonic pretreatment greatly enhanced substrate mass transfer, further reducing the esterification time. The max conversion rate 94.72% of phytosterol was obtained after 9 h reaction under optimum condition (the molar ratio of oleic acid to phytosterol was 6:1, the concentration of CRL-FIL-CLEAs@Fe 3 O 4 was 10 wt% of the phytosterol mass). After five recycles, the activity of CRL-FIL-CLEAs@Fe 3 O 4 (80.02%) was still 2.68 times higher than that of natural lipase system (29.91%). Meanwhile, the novel immobilized lipase (CRL-FIL-CLEAs@Fe 3 O 4 ) before and after reaction was characterized by SEM, AFM, VSM, TEM, and TGA. The results showed that CRL-FIL-CLEAs@Fe 3 O 4 was a robust and recyclable biocatalyst for phytosterol esterification.
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FOOD CHEMISTRY
·
2026
·
IF 9.8
Shengli Ding,Mengqi Wang,Guiqing Lin,Yanrong Song,Ji Zhang,Yufei Zhang,Mingming Zheng
Inspired by the natural crystal evolution trajectory of corals, this study introduces a mild two-step “defective pre-growth/crystallization” strategy to in situ encapsulate Candida antarctica lipase B (CaLB) within covalent organic frameworks (COFs). Rapidly formed amorphous polymer microspheres serve as the core skeletal structure. Upon enzyme adsorption onto their surfaces, these microspheres undergo crystalline readjustment to embed the enzymes and form a protective exoskeleton. The resulting CaLB@TPB-TFPB COF-I biocatalyst demonstrates superior thermal stability, organic solvent tolerance, and reusability compared to both free lipase and commercial Novozym 435. It achieves a 95.7% conversion rate for caproic acid esterification under anhydrous conditions and maintains over 90% conversion efficiency across seven consecutive cycles. This work also elucidates the multiple critical roles of water in enzymatic ester synthesis. This coral-inspired encapsulation approach leverages the tunable properties of COFs to enhance enzyme performance, offering an efficient solution for the biocatalytic synthesis of flavor esters.
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JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
·
2017
·
IF 3.154
Shi-Lin Cao,Xiao Deng,Pei Xu,Zi-Xuan Huang,Jian Zhou,Xue-Hui Li,Min-Hua Zong,Wen-Yong Lou
A novel deep eutectic solvent (DES)–DMSO cosolvent system has been, for the first time, successfully used as the reaction medium for the enzymatic acylation of dihydromyricetin (DMY) catalyzed by the immobilized lipase from Aspergillus niger (ANL). The cosolvent mixture, ChCl:Glycerol–DMSO (1:3, v/v) proved to be the optimal medium. With the newly developed cosolvent, the initial reaction rate of enzymatic acylation of DMY achieved 11.1 mM/h and the conversion of DMY was 91.6%. ANL@PD-MNPs is stable and recyclable in this cosolvent, offering 90% conversion rate after repeated use of 5 times. The lipid-solubility of DMY-16-acetate was 10 times higher than that of its raw materials DMY. The results showed that the DMY-16-acetate product exhibits good antioxidative activity. The present research illustrated that the use of DES–DMSO cosolvent may become a feasible alternative for the synthesis of DMY ester.
研究领域:
生物催化
·
绿色化学
·
酶工程
·
药物化学
·
天然产物化学
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ANALYTICA CHIMICA ACTA
·
2026
·
IF 6
Mengxue Tang,Jiale Zhang,Qixuan Mu,Keyan Chen,Yibing Ji
Background Enantiomers may have differences in biological effects, pharmacological activity, and toxicity. Currently, global regulatory authorities are imposing increasingly stringent approval requirements for single-enantiomer drugs. Coupled with the continued growth of the chiral pharmaceutical market, this makes the development of chiral separation technology an urgent scientific task. Therefore, the separation and analysis of chiral drug enantiomers are directly related to human health. Enzyme-based chiral stationary phase (CSP) is a promising platform. Unfortunately, the fragility of natural enzymes, as well as the complexity and low efficiency of the preparation process, hinder their practical application in chiral separation. Results Metal organic frameworks (MOFs), which have enormous potential in the fields of enzyme immobilization and capillary electrochromatography (CEC) separation, were explored as support materials with good enzyme immobilization performance and CSP with separation abilities. Lipase (from porcine pancreatic) was encapsulated into a metal organic framework (MOF) under the concept of "in situ". Effective enzyme loading capacity enables composite materials (Lipase@HKUST-1) to inherit lipase's natural chiral recognition ability. On this basis, inspired by the same concept, Lipase@HKUST-1 was directly grown in the open column for capillary electrochromatography (CEC). By optimizing the interface combination method and simplifying the column preparation steps, the efficiency and performance of capillary column preparation have been effectively improved. Enantiomer separation of multi-chiral drugs such as naproxen and chlorpheniramine has been achieved. Theoretical calculations further explore potential chiral recognition mechanisms. Significance The effective combination of cost-effective lipase (from porcine pancreatic) and MOF materials enriches the library of chiral materials for enantioseparation. The understanding of the chiral recognition mechanism inspires the design of ideal performance materials. The highly stable MOF separation platform for biological functions has introduced a pioneering research paradigm for the CSP development of OT-CEC.
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MACROMOLECULAR BIOSCIENCE
·
2026
·Vol. 26
·期 8
·e70238
·
IF 4.2
Meng Wang,Hongzhen Jia,Chengfu Zhang,Ningli Wang,Puzhao Liu,Dong Pei,Qingli Qu
Enzyme immobilization is an effective strategy to improve catalyst recovery and operational stability, but conventional approaches are often limited by diffusion resistance, steric hindrance, and insufficient control over the enzyme microenvironment. Hydrogel-based materials are attractive supports because their hydrated, tunable, and porous networks help preserve enzyme conformation while improving substrate diffusion and mass transfer. Here, a gas-shearing microfluidic strategy was developed to fabricate alginate/chitosan hydrogel microreactors for dual-mode lipase immobilization through entrapment and genipin-mediated covalent binding. By tuning gas-liquid shear, microspheres with controllable and narrow size distribution were generated without surfactants or UV-initiated polymerization. Importantly, genipin was introduced as a mild and biocompatible cross-linker to reinforce the alginate/chitosan network and create a stable interfacial microenvironment for enzyme immobilization. Compared with conventional cross-linkers, the milder and more controllable reactivity of genipin is advantageous in preserving enzyme conformation and catalytic performance. The resulting microreactors exhibited enhanced catalytic activity, improved storage stability, and good reusability. After five consecutive cycles, the entrapped and covalently immobilized systems retained 70% and 81% of their initial activity, respectively. These results demonstrate that gas-shearing microfluidics combined with genipin-mediated network reinforcement provides a robust and biocompatible platform for constructing hydrogel-based enzymatic microreactors with improved catalytic performance and operational durability.
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