INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
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2018
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IF 3.909
Yue Li,Nanjing Zhong,Ling-Zhi Cheong,Jianrong Huang,Hongxiao Chen,Shaoyan Lin
In this study, SBA-15 was modified by a series of silane coupling reagents and later used to immobilize Candida antartica lipase B (CALB). The enzymatic properties of the immobilized CALB samples were studied. In addition, the catalytic performance in glycerolysis of soybean oil for diacylglycerols (DAG) production was also investigated. The highest enzymatic activity up to 6100.00 ± 246.41 U/g was observed from the propyl methacrylate group modified SBA-15 supported CALB. No loss of activity was observed from the propyl methacrylate group modified SBA-15 supported CALB, but a higher-than-initial activity was notably found from 3-aminopropyl group and n -octyl group modified SBA-15 supported CALB after a 4-h incubation in air at 70 °C. 1-isocyanatopropane group modified SBA-15 supported CALB exhibited selectivity for DAG production. DAG content up to 61.90 ± 2.38 wt% and a DAG/MAG ratio at 3.11 ± 0.08 was obtained after a 24-h reaction at 60 °C in a solvent-free system.
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ENZYME AND MICROBIAL TECHNOLOGY
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2014
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IF 2.966
Chuan-Yang Shang,Wei-Xun Li,Rui-Feng Zhang
ZnO nanowires were successfully introduced into a macroporous SiO 2 by in situ hydrothermal growth in 3D pores. The obtained composites were characterized by SEM and XRD, and used as supports to immobilize Candida antarctica lipase B (CALB) through adsorption. The high specific surface area (233 m 2 /g) and strong electrostatic interaction resulted that the average loading amount of the composite supports (196.8 mg/g) was 3–4 times of that of macroporous SiO 2 and approximate to that of a silica-based mesoporous material. Both adsorption capacity and the activity of the CALB immobilized on the composite supports almost kept unchanged as the samples were soaked in buffer solution for 48 h. The chiral resolution of 2-octanol was catalyzed by immobilized CALB. A maximum molar conversion of 49.1% was achieved with 99% enantiomeric excess of ( R )-2-octanol acetate under the optimal condition: a reaction using 1.0 mol/L ( R , S )-2-octanol, 2.0 mol/L vinyl acetate and 4.0 wt.% water content at 60 °C for 8 h. After fifteen recycles the immobilized lipase could retain 96.9% of relative activity and 93.8% of relative enantioselectivity .
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EUROPEAN JOURNAL OF LIPID SCIENCE AND TECHNOLOGY
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2015
·Vol. 117
·期 10
·1636-1646
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IF 1.812
Lingyi Liu,Meirong Pang,Ying Zhang
AOB-w is a water-soluble antioxidant extracted from bamboo leaves, containing four flavone C-glucosides (orientin, isoorientin, vitexin, and isovitexin) as functional components. Flavone C-glucoside esters were firstly synthesized by three lipases (CALB, RM IM, and TL IM) in organic solvent system or solvent-free system. Results indicated that C12 fatty acid ester exhibited the optimal antioxidant capacity, CALB was the most efficient lipase in both systems, and higher conversion yields were achieved in solvent-free system. Highest conversion was obtained with 1% water content for CALB and 2% water content for RM IM and TL IM. All lipases displayed absolute 6″-regioselectivities with monoester. It is required to consider both of hydrophobicity and antioxidant capacity to prepare high-efficiency oil-soluble antioxidant. Regression equations were built up to illuminate the relationship between conversion yield of flavone C-glucoside and antioxidant capacity of its corresponding ester. Highest antioxidant capacity could be achieved when conversion yield was nearly 60% for flavone C-glucosides. Based on reaction parameters of flavone C-glucosides, high-efficiency eAOB-o was prepared, which could be expected as an excellent oil-soluble antioxidant in lipids. Practical applications: Water-soluble antioxidant of bamboo leaves (AOB-w) is a natural food antioxidant extracted from bamboo leaves, with four flavone C-glucosides (orientin, isoorientin, vitexin, and isovitexin) as functional components. This study aimed to provide a practical procedure to prepare high-efficiency lipid antioxidant by enzymatic acylation. Based on the optimal parameters from the synthesis of flavone C-glucoside esters, high-efficiency oil-soluble antioxidant of bamboo leaves (eAOB-o) was prepared. eAOB-o exhibited higher antioxidant capacity than cAOB-o, which has been approved as food antioxidants in China. High-efficiency acylation products were obtained by consideration both of lipid solubility and antioxidant capacity. Based on the rule, flavone C-glucoside ester and eAOB-o were prepared.
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KOREAN JOURNAL OF CHEMICAL ENGINEERING
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2016
·Vol. 33
·期 2
·610-615
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IF 1.408
Cui Jian Dong,Liu Rong Lin,Li Lin Bo
Cross-linked enzyme aggregates from bovine pancreatic lipase were prepared by co-aggregation of lipase and BSA (Lipase-BSA-CLEAs). The main factors in the preparation of lipase-BSA-CLEAs were optimized. The highest activity recovery was around 75% under the condition of using 1% (v/v) glutaraldehyde as cross-linker and 0.05 g/L bovine serum albumin as feeder for 2 h cross linking. The optimum temperature for both lipase-CLEAs and lipase- BSA-CLEAs was measured as 60 °C, which is 10 °C higher than that of free lipase. Moreover, the lipase-BSA-CLEAs evidenced higher thermal stability and excellent reusability in comparison with the lipase-CLEAs. Lipase-BSA-CLEAs retained more than 75% of the initial activity after eight cycles of reuse, while lipase-CLEAs only retained 20% of its initial activity. Additionally, lipase-BSA-CLEAs showed more storage stability than free lipase and lipase-CLEAs. The high stability and recyclability of lipase-BSA-CLEAs make it efficient for different industrial applications.
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JOURNAL OF CHEMICAL TECHNOLOGY AND BIOTECHNOLOGY
·
2016
·Vol. 92
·期 7
·1785-1793
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IF 2.738
Jiandong Cui,Tao Lin,Yuxiao Feng,Zhilei Tan,Shiru Jia
BACKGROUND Cross-linking enzyme aggregates (CLEAs) seem to be a promising immobilization method due to mild processing conditions and short preparation time. However, the CLEAs prepared in aqueous solution exhibit amorphous large clusters that cause significant mass-transfer limitations, leading to low catalytic efficiency. In this work, novel spherical CLEAs of lipase from bovine pancreas (spherical CLEAs) were prepared within droplets dispersed in a water-in-hydrophobic ionic liquid microemulsion rather than a conventional aqueous solution. The properties of the spherical CLEAs were determined. RESULTS The resultant CLEAs exhibited spherical structure with good monodispersity instead of the amorphous clusters of conventional CLEAs, and showed higher activity recovery (84.6%) than that of conventional CLEAs (52.8%). The high activity recovery of spherical CLEAs could be attributed to both interfacial activation of the microemulsion system and the well-defined structure of the spherical CLEAs, which not only activated lipases in an active form, but also decreased mass-transfer limitations. Moreover, the thermostability, storage stability, tolerance against hydrophilic solvents, and mechanical stability of the spherical CLEAs were enhanced significantly. The spherical CLEAs evidenced excellent reusability in comparison with conventional CLEAs. CONCLUSIONS The novel strategy in this study might open an attractive way towards effectively improving the catalytic properties of traditional CLEAs. © 2016 Society of Chemical Industry
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BIORESOURCE TECHNOLOGY
·
2024
·
IF 9.7
Shuo Zou,Jiena Chen,Yee-Ying Lee,Yong Wang,Zhen Zhang
Partial acylglycerols are valued for their emulsifying and stabilizing properties, yet precise green synthesis remains challenging due to low yield and selectivity. This study aimed to elucidate the “lipase selectivity-substrate structure-product composition” relationship to enhance the yield of targeted partial acylglycerol. The results showed that lipase exhibited a greater selectivity towards fatty acids with shorter chain lengths and higher unsaturation. Hydroxyl donors also affected the esterification process, with the enzyme-acyl complex exhibiting selectivity towards hydroxyl donors as follows: glycerol > monoacylglycerol > diacylglycerol. Substrate ratio significantly influenced enzymatic reactions; a 10:1 ratio favored triacylglycerol formation (>80 %), while a 1:1 ratio produced > 90 % partial acylglycerols. Molecular docking simulations revealed that substrates primarily interacted with lipase through hydrogen bonding and hydrophobic interactions. A comprehensive understanding of lipase selectivity patterns could facilitate the design of more efficient reaction systems, enabling the conversion of basic lipid resources into desired high value-added products.
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ACS Sustainable Chemistry & Engineering
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2024
·
IF 7.1
Zeqing Liu,Lingmei Dai,Dehua Liu,Wei Du
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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FOOD CHEMISTRY
·
2024
·
IF 8.5
Weiyan Guan,Juan Cheng,David Julian McClements,Zongcai Tu,Jing Chen,Da Ma
2,4-di-tert-butylphenol (2,4-DTBP) is an additive used in food packaging. The inhibitory effects of 2,4-DTBP on pancreatic lipase (PL) were investigated in this study. Kinetic analysis indicated that 2,4-DTBP competitively and reversibly inhibited PL activity. At 4.85 mM, PL activity decreased by 35.5 ± 1.6 %. 2,4-DTBP quenched the fluorescence of PL by hydrogen bonding and van der Waals forces. Circular dichroism spectroscopy showed that 2,4-DTBP induced changes in the secondary structure of PL. Molecular docking revealed that 2,4-DTBP interacted with Phe77, Leu153, and Ser152 residues of PL, which account for suppressing lipid hydrolysis. An in vitro digestion study showed that 2,4-DTBP inhibited the digestion of lipid in oil-in-water emulsions. This study improved our understanding of the effects of 2,4-DTBP on digestive enzyme. It also underscored the need for better monitoring and control of the leaching of this additive from packaging materials into foods.
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FOOD CHEMISTRY
·
2025
·
IF 9.8
Shuo Zou,Zhen Zhang,Yee-Ying Lee,Hongzeng Ai,Yufei Zhang,Yong Wang
Acylglycerols are widely used in the food industry due to their antimicrobial, emulsifying and nutritional properties. This study investigated the key reaction parameters, mass transfer mechanisms, and kinetic features of lipase-catalyzed esterification in a solvent-free system. Taguchi method was further employed to explore the relationship between “reaction parameter - yield composition”. The results revealed that the maximum selectivity were achieved fror MAG (57.72 %), DAG (82.67 %) and TAG (79.29 %) under different enzymatic conditions. Fatty acid-to-glycerol molar ratio had the greatest impact on DAG selectivity, contributing 38.08 % of total impact level. Mass transfer analysis showed that external mass transfer limitation could be effectively overcome at stirring speeds above 600 rpm. Kinetic analysis confirmed that the reaction followed the Ping-Pong Bi Bi mechanism with alcohol and acid inhibition (SSE = 0.000643). This work provided a theoretical basis for developing more efficient and selective catalytic processes, aiding in quality control, reactor design, and industrial scale-up.
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SCIENCE OF THE TOTAL ENVIRONMENT
·
2017
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IF 4.9
Rui Zhang,Yang Liu,Xinran Huang,Mengchen Xu,Rutao Liu,Wansong Zong
The extensive use of surfactants in food, laundry products and agriculture has caused concern about their biosafety. However, few studies have been done on their potential effect on the lipase which has always been used with surfactants in food and laundry industry. Herein, we investigated the interaction of three surfactants (sodium dodecyl sulfate (SDS), sodium dodecyl benzene sulfonate (SDBS), sodium lauryl sulfonate (SLS)) with Candida rugosa lipase (CRL), which is a popular biocatalyst used regularly with surfactants. The effect of the three surfactants on the conformation and activity of CRL was evaluated by using multiple spectral methods, enzyme activity assay and molecular docking modeling. The results demonstrated that CRL interacted with SDS, SDBS and SLS primarily through hydrophobic forces, H-bonding and electrostatic forces, respectively. The binding constants (K A ) of SDBS with CRL varied with temperature: 1.99 × 10 3 mol/L at 298 K and 4.13 × 10 3 mol/L at 318 K. SDS and SDBS affected the secondary structure and skeleton of CRL, which changed the polarity of CRL and enhanced its activity. SLS also changed the secondary structure and activity of CRL moderately, but had little effect on its polarity and chromophore microenvironment. Accordingly, all three surfactants exhibited effect to CRL on the molecular level calling for more attention to pay on their biosafety. The work demonstrates that SDS, SDBS and SLS could cause negative effects to CRL from different angles and therefore are not bio-friendly detergents.
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JOURNAL OF MOLECULAR LIQUIDS
·
2024
·
IF 5.3
Yu Chen,Xirong Huang
CHAPS (3-[(3-cholamidopropyl) dimethylammonio]-1-propane sulfonate), a biocompatible zwitterionic surfactant derived from bile salt, has attracted great attention due to its distinct molecular structure and aggregation behavior. Addition of a low level of CHAPS to AOT (sodium bis(2-ethylhexyl) sulfosuccinate) reverse micelles has been found to be able to enhance the catalytic activity of the solubilized lipase. In this study, the effect of CHAPS on the lipase-catalyzed selective synthesis of (S)-n-octyl ibuprofen ester was investigated in AOT reverse micelles at 37 °C. The results demonstrate that the presence of CHAPS in AOT reverse micelle enhances both the yield and the enantiomeric excess (ee) value of (S)-n-octyl ibuprofen ester, especially at low water content. With 8 mM CHAPS in AOT reverse micelle ([AOT] = 100 mM, [H 2 O]/[AOT] = 12, pH = 7.0), a 48-hour yield of 34.2 % could be obtained, which is approximately twice that without CHAPS. In addition, the ee value of the product is increased from 89.1 % to 98.2 %. To understand the mechanism of the CHAPS effect, dynamic light scattering, fluorescence emission spectroscopy and Fourier transform infrared spectroscopy techniques were used to characterize the size of the reverse micelle, the conformation of the solubilized lipase and the activity of the bulk water in the reverse micelle. It reveals that at low water content, the addition of CHAPS enlarges the size of AOT reverse micelle, stabilizes the lipase conformation and reduces the nucleophilicity of bulk water in AOT reverse micelle. The synergistic effect of the aforementioned factors results in the improvement of the enzymatic synthesis of the ester. The above research provides scientific support for the lipase-based preparation of chiral acids/alcohols in the reverse micellar system.
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FOOD CHEMISTRY
·
2018
·
IF 4.946
Nanjing Zhong,Weilin Chen,Liyan Liu,Hongxiao Chen
In this study, mesoporous silica SBA-15 was modified by organic functional groups through silanization. Series of organosilane compounds were grafted onto the SBA-15, and the obtained functionalized carriers were then used to immobilize the lipase from Rhizomucor miehei (RML). The enzymatic properties of the obtained immobilized RML samples were evaluated, and the catalytic efficiencies in glycerolysis of triacylglycerols (TAG) reaction were studied. Compared with the parent SBA-15 immobilized RML, the organic modification gave a maximum improvement of enzymatic activity from 200.00 to 13211.11 U/g; in addition, TAG conversion and diacylglycerols (DAG) content increased from 21.28 to 84.24% and 15.45 to 59.03% respectively. The organic modification also decreased the sensitivity of immobilized RML in extreme pH values and increased their thermostability.
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