JOURNAL OF FOOD SCIENCE
·
2025
·Vol. 90
·期 5
·e70302
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IF 3.4
Pengfei Zhou,Hui Fang,Zhihao Zhao,Guang Liu,Jiarui Zeng,Yuanyuan Deng,Mingwei Zhang
The precise regulation of enzyme conformation through the immobilization of enzymes on carriers using sewing techniques represents a key focus in the site-specific chemically modification engineering. Lipase-mediated enzymatic interesterification (EIE) is of considerable significance in lipid chemistry, having demonstrated substantial potential in the modification of lipids. In this study, we developed an innovative nanomaterial Fe 3 O 4 -SiO 2 -APTES for site-specific immobilization of Thermomyces lanuginosus lipase (TLL), achieving an immobilization yield of 51.98% and an enzyme loading capacity of 123.18 mg/g. The specific activity of the enzyme was 1034.09 U/g following lyophilization, representing increases of 2.6-fold compared to free TLL. The as-prepared biocatalyst TLL@Fe 3 O 4 -SiO 2 -APTES exhibited enhanced catalytic activity, remarkable tolerance to organic solvents, substrate selectivity, and recyclability over multiple cycles. Rice bran oils (RBO) and palm stearin (PS) were employed as substrates for EIE, yielding oils with better performance of solid fat content (SFC), crystallization rate, and thermodynamic properties compared to those of physical blending oils. Additionally, we investigated the catalytic mechanism of EIE using molecular docking analysis. The present study provides a theoretical foundation for the application of immobilized lipase as biocatalysts in food industrial settings. Practical Application : TLL@Fe 3 O 4 -SiO 2 -APTES, modified at specific sites using nanomaterials, not only enhances the catalytic efficiency of the enzyme but also facilitates its reuse across multiple batches. This fixed enzyme could effectively catalyze the transesterification between PS and RBO, resulting in high-quality of oils specifically designed for baking foods. The findings in this study provide valuable guidance for the green processing of oils and fats.
研究领域:
食品科学
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生物化学
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酶工程
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DOI
PubMed
高影响因子
COLLOIDS AND SURFACES B-BIOINTERFACES
·
2024
·
IF 5.4
Ting Feng,Jiani Shi,Jiaojiao Xia,Xuemei Ren,Onyinye Idowu Adesanya,Hongbo Suo,Bin Zou
In this study, the critical importance of designing an appropriate immobilized carrier and method for free lipase to ensure exceptional biological catalytic activity and stability was emphasized. Covalent organic frameworks (COF-1) were synthesized as a novel porous carrier with an azine structure (-C N-N C-) through the condensation of hydrazine hydrate and benzene-1,3,5-tricarbaldehyde at room temperature. Simultaneously, Rhizomucor miehei lipase (RML) was immobilized within the COF-1 carrier using an in-situ aqueous phase method. Characterization of the carrier and RML@COF-1 and evaluation of the lipase properties of RML and RML@COF-1 through p -Nitrophenyl palmitate hydrolysis were conducted. Additionally, application in the synthesis of 1, 3-dioleoyl-2-palmitoylglycerol (OPO) was explored. The results showed that RML@COF-1 exhibited a high enzymatic loading of 285.4 mg/g. Under 60℃ conditions, the activity of RML@COF-1 was 2.31 times higher than that of free RML, and RML@COF-1 retained 77.25% of its original activity after 10 cycles of repeated use, indicating its excellent thermal stability and repeatability. Under the optimal conditions (10%, 1:8 PPP/OA, 45℃, 5 h), the yield of OPO reached 47.35%, showcasing the promising application prospects of the novel immobilized enzyme synthesized via in-situ aqueous phase synthesis for OPO preparation.
研究领域:
生物化学
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酶工程
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材料科学
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产品关联
DOI
PubMed
高影响因子
PROCESS BIOCHEMISTRY
·
2024
·
IF 3.7
Hongbo Suo,Xinzheng Liu,Shu Chen,Qi Li,Xiangnan Liu,Lili Xu
Biodiesel is more environmentally friendly compared to traditional petroleum diesel. The method of producing biodiesel catalyzed by lipases, as a green chemistry technology, can further reduce its negative impact on the environment. In this work, lipase immobilized on magnetic cellulose was embedded in Cu(PABA), and then the biocomposite (MCL@Cu(PABA)) was used for biodiesel production. The good biocompatibility and flexible skeleton structure of cellulose can buffer the compression effect on enzyme molecules during the formation of Metal-Organic Frameworks (MOFs), and the MOFs protective layer can reduce the damage caused by denaturants to enzyme molecules. The biocatalyst showed enhanced activity and stability with a lower deactivation constant ( K d ). Under the optimized reaction conditions, the biodiesel yield can reach 78.4 %. After reused for 7 times, the biocatalyst can still achieve a biodiesel yield of 58.8 %. Moreover, after stored for 30 days, the biodiesel yield can still reach 70.3 %. For all experimental yields, the standard deviation (SD) ranged from 2.4 % to 4.5 %. Secondary structure analysis showed that the rigid structure and active conformation of lipase was enhanced after Cu(PABA) encapsulation.
研究领域:
生物化学
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环境科学
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产品关联
DOI
高影响因子
ENZYME AND MICROBIAL TECHNOLOGY
·
2019
·
IF 3.553
Yue Zhang,Wenhui Sun,Nora Mohamed Elfeky,Yuepeng Wang,Dongying Zhao,Hao Zhou,Jingyun Wang,Yongming Bao
Lipase ZC12, a cold-adapted lipase derived from Psychrobacter sp. ZY124, can be effectively activated by Ca 2+ . Inspired by this significant property, we developed a novel immobilized lipase ZC12/Ca 3 (PO 4 ) 2 hybrid nanoflowers (LHNs). The LHNs have been characterized as a regular hierarchical flowerlike structure nanoflowers by scanning electron microscopy (SEM). Compared with free lipase ZC12, the LHNs exerted enhanced enzymatic activity of 206% and 2.31-fold in k cat / K m value, especially high specific activity at low temperature. After 7 successive cycles, the LHNs could still maintain its initial activity, demonstrating superior durability than the free lipase ZC12. Meanwhile, its stability basically kept unchanged in a wide range of temperature and pH. Finally, fructose laurate was transformed by the LHNs with 57.39% conversion rate which is twice as much as the free lipase. To sum up, these results validated that LHNs could emerge as an efficient immobilized lipase and possess the promising potential for practical applications.
研究领域:
生物化学
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酶工程
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产品关联
DOI
PubMed
高影响因子
Food Bioscience
·
2024
·
IF 4.8
Ji Wang,Xu-Hui Huang,Xusong Wang,Hehe Tian,Liang Wang,Da-Yong Zhou,Lei Qin
Flavor is one of the important sensory attributes of foods. This research explored the effect of lipase on flavor, lipid composition, lipase activity, lipid oxidation, and sensory evaluation of lightly salted large yellow croaker. Results exhibited that the addition of lipase improved the reduced-salt product's flavor. The content of 1-octen-3-ol, nonanal, 2,5-octanedione, hexanal, heptanal, and octanal were key aromas and were increased by the addition of lipase. Through adding the lipase, triacylglycerol (TG) and phosphatidylethanolamine (PE) and could be decompose into fatty acids. Products marinated in 4% NaCl coupled with lipase exhibited higher thiobarbituric acid reactive substance (TBARS) values, acid values, and lipase activity compared with those marinated in 4% NaCl. Moderate promotion of lipid oxidation is beneficial for improving product flavor. Lipase addition had a positive influence on saltiness, aroma, and over-acceptability of reduced-salt products by multi-sensory synergy perception. Especially, addition of 0.2% or 0.4% lipase to reduced-salt products is closest to the flavor profile of normal-salt products. These results provide a new insight into improving reduced-salt foods.
研究领域:
食品科学
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生物化学
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产品关联
DOI
高影响因子
STARCH-STARKE
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2021
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IF 2.741
Hui Yang,Rihui Lin,Yanye Fan,Sai Jiang,Yujiao Lin
The rosin acid starch (RAS) is prepared under the catalysis of lipase, by esterification on the starch particles' surface in a two-phase reaction system, using rosin acid and native cassava starch as starting materials. The effects of reaction time, solvent types, substrate ratio, reaction temperature, and lipase dosage on the degree of substitution (DS) of RAS are investigated. Based on the single factor experiments, the reaction conditions are optimized according to the principle of the combination Box-behnken centered design and response surface methodology analysis. The mathematical model of the influence of reaction temperature, material ratio, and enzyme addition amount on DS is established. The optimum synthesis conditions are determined as follows: solvent, trichloromethane; reaction time, 10 h; reaction temperature, 59 °C; substrate ratio (m Rosin acid :m starch) , 4.1; and lipase dosage, 264 µL. Under these conditions, it is found that the DS is 0.0608. The analysis of variance and verification experiments show that the mathematical model has good fit degree and high credibility. Compared with the native cassava starch, RAS has improved contact angle, emulsion capacity, and emulsion stability.
研究领域:
食品科学
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生物化学
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产品关联
DOI
高影响因子
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
·
2013
·Vol. 171
·期 7
·1559-1567
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IF 1.893
Wang Na,Zhang Wei,Zhou Long-Hua,Deng Qing-Feng,Xie Zong-Bo,Yu Xiao-Qi
A facile tandem route to α,β-unsaturated aldehydes was developed by combining the two catalytic activities of the same enzyme in a one-pot strategy for the aldol reaction and in situ generation of acetaldehyde. Lipase from Mucor miehei was found to have conventional and promiscuous catalytic activities for the hydrolysis of vinyl acetate and aldol condensation with in situ formed acetaldehyde. The first reaction continuously provided material for the second reaction, which effectively reduced the volatilization loss, oxidation, and polymerization of acetaldehyde, as well as avoided a negative effect on the enzyme of excessive amounts of acetaldehyde. After optimizing the process, several substrates participated in the reaction and provided the target products in moderate to high yields using this single lipase-catalyzed one-pot biotransformation.
研究领域:
生物化学
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酶工程
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产品关联
DOI
PubMed
高影响因子
LWT-FOOD SCIENCE AND TECHNOLOGY
·
2023
·
IF 6
Yujie Chen,Ruhui Liu,Jingyan Li,Yanjie Wang,Chunfeng Guo,Xin Lü
1-Oleoyl-2-palmitoyl-3-linoleoylglycerol (OPL) is the most abundant triacylglycerol (TAG) molecule in Chinese human milk. The selectivity of three lipases including Rhizomucor miehei lipase (RML), Thermomyces lanuginose lipase (TL), and Candida antarctica lipase (CALB) in OPL synthesis were evaluated. The effects of different reaction conditions on selectivity were first investigated. Unexpectedly, the three sn -1,3 regioselectivity lipases, also have selectivity for the structure of product TAGs. Compared with symmetric TAGs, lipases had poor selectivity toward asymmetric OPL. Furthermore, molecular simulations were used to deeply understand the molecular factors affecting lipase selectivity. The results showed that hydrophobic interactions, lipases lid domain flexibility, and the stability of hydrogen bonds between lipases and TAGs were the main molecular factors responsible for the selectivity of lipases.
研究领域:
生物化学
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食品科学
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产品关联
DOI
高影响因子
JOURNAL OF MATERIALS SCIENCE
·
2023
·
IF 4.5
Gao Nengwen,Liu Jing,Wang Xiaoli,Zhang Yu
Lipases are widely used in industry. Free lipases are difficult to recover and have poor stability under operational conditions. Herein, lipases are immobilized onto the methyltrimethoxysilane (MTMS)-modified ceramic membranes (~ 5 nm) with reverse filtration method, and further cross-linking by glutaraldehyde (GA) is used to improve the lipase stability. FTIR and XPS analyses demonstrate the successful immobilization of lipase. The immobilized lipases are used to hydrolyze glycerol triacetate (GT) to fatty acids and glycerol. Under the optimal immobilization conditions (MTMS concentration 0.1 M, lipase immobilization time 80 min, lipase concentration 3 mg/mL, and GA concentration 2%), the loading of lipases reaches 0.24 mg/g. Under the optimal operational conditions (temperature 45 °C, pH 7, pressure 0.2 MPa, GT concentration 0.05 M), the immobilized lipases have the highest catalytic activity of 25 U/mg. Moreover, the thermal and pH stabilities of immobilized lipases are found to be higher than those of the free lipases. In the long-term runs, the immobilized lipases still have 64% of the initial activity after 7 cycles, indicating good reusability. This paper provides a simple process for immobilizing lipase on ceramic membranes. The immobilized lipases have better stability at high temperature and basic environments (pH 7–9), which would have broad applications in lipase-catalyzed reactions. Graphical Abstract
研究领域:
生物化学
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酶工程
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DOI
高影响因子
JOURNAL OF BIOTECHNOLOGY
·
2015
·
IF 2.871
Wei Li,Huan Wu,Benguo Liu,Xuedan Hou,Duanji Wan,Wenyong Lou,Jian Zhao
Dihydromyricetin is the principle component of the Chinese herbal tea Teng-cha and a promising ingredient for functional food and nutraceuticals, but its low solubility limits its application potentials. This study explored enzymatic acylation of dihydromyricetin to improve its solubility in lipid systems. Acylation was achieved with several lipases with the synthesis of a major (>86%) product and a minor product. Isolation and purification of the products by preparative HPLC followed by LC–MS, 13 C NMR, 1 H NMR and 2 D-HSQC NMR analyses showed that the major product was a dihydromyricetin monoester with the acylation site at the 3-OH group of C ring. Quantum chemical calculations revealed that the 3-OH had the lowest antioxidant activity , and therefore acylation at this site was expected to have minimum impact on the antioxidant activity. Several factors, including solvent, acyl donor, enzyme origin, molar ratio of substrates and reaction temperature and time, exhibited significant effects on the initial rate, conversion yield and regioselectivity of the reaction. Acylation occurred only with vinyl acetate as the acyl donor, and highest conversion yields were achieved with immobilized Penicillium expansum lipase and Novozyme 435 with DMSO and acetonitrile being the best solvents. In general, the acylation results were found to be superior to previous reports on acylation of aglycone flavonoids with respects to conversion yield and regioselectivity.
研究领域:
生物化学
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食品科学
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药理学
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DOI
PubMed
高影响因子
ENZYME AND MICROBIAL TECHNOLOGY
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2015
·
IF 2.322
Xuemei Tian,Suoqin Zhang,Liangyu Zheng
The first Novozym 435 lipase-catalyzed Morita–Baylis–Hillman (MBH) reaction with amides as co-catalyst was realized. Results showed that neither Novozym 435 nor amide can independently catalyze the reaction. This co-catalytic system that used a catalytic amount of Novozym 435 with a corresponding amount of amide was established and optimized. The MBH reaction strongly depended on the structure of aldehyde substrate, amide co-catalyst, and reaction additives. The optimized reaction yield (43.4%) was achieved in the Novozym 435-catalyzed MBH reaction of 2, 4-dinitrobenzaldehyde and cyclohexenone with isonicotinamide as co-catalyst and β-cyclodextrin as additive only in 2 days. Although enantioselectivity of Novozym 435 was not found, the results were still significant because an MBH reaction using lipase as biocatalyst was realized for the first time.
研究领域:
生物化学
·
催化反应
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产品关联
DOI
PubMed
高影响因子
PROCESS BIOCHEMISTRY
·
2021
·
IF 3.757
Wenfeng Zhou,Xiaohong Zhou,Wei Zhuang,Rijia Lin,Ye Zhao,Lei Ge,Ming Li,Jinglan Wu,Pengpeng Yang,Hongman Zhang,Chenjie Zhu,Hanjie Ying
To effectively immobilize an enzyme while maintaining its high activity and stability, the design of supports with controlled geometric structures and heterogeneous surface properties is desirable. Towards this goal, heterogeneous titanium dioxide (TiO 2 ) surfaces with controlled pore sizes were synthesized in this study and used to efficiently immobilize lipase. The immobilized lipase activity increased by a factor of 1.31 with an increase in the TiO 2 pore size from 11.46 to 21.14 nm. The highest protein loading of 15.52 mg/g was achieved in ethenyl triethoxy silane (ETS)-modified TiO 2 (E-P25) after immobilizing the enzymes at 30 ℃, pH 7.33 for 3 h and using a protein concentration in solution of 0.176 mg/mL. Among the different surface functionalities, the highest activity yield of 428.04 % was accomplished by using TiO 2 calcinated at 650 ℃ and modified by ETS as immobilization support. The immobilized enzymes showed excellent storage stability and retained almost 95 % of their activity after being stored at 4 ℃ for 8 weeks. This research provides experimental evidence that highlights the importance of studying of enzyme immobilization on the supports with synergistically designed geometric structures and surface chemical properties.
研究领域:
生物化学
·
材料科学
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产品关联
DOI
高影响因子
危险品化学品经营许可证（带存储）