Suitability of Recombinant Lipase Immobilised on Functionalised Magnetic Nanoparticles for Fish Oil Hydrolysis

Verma, Madan L.; Rao, Nalam Madhusudhana; Tsuzuki, Takuya; Barrow, Colin J.; Puri, Munish

doi:10.3390/catal9050420

Cited by 47 publications

(8 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The temperature is an important parameter for the properties of enzymes [49,50,51,52]. The DFF yield was studied as a function of temperature ranging from 15–45 °C.…”

Section: Resultsmentioning

confidence: 99%

Co-Immobilization of Tri-Enzymes for the Conversion of Hydroxymethylfurfural to 2,5-Diformylfuran

Shi

et al. 2019

Molecules

View full text Add to dashboard Cite

Acting as a “green” manufacturing route, the enzyme toolbox made up of galactose oxidase, catalase, and horseradish peroxidase can achieve a satisfactory yield of 2,5-diformylfuran derived from 30 mM hydroxymethylfurfural. However, as the concentration of hydroxymethylfurfural increases, the substrate causes oxidative damage to the activity of the tri-enzyme system, and the accumulated hydrogen peroxide produced by galactose oxidase causes tri-enzyme inactivation. The cost of tri-enzymes is also very high. These problems prevent the utilization of this enzyme toolbox in practice. To address this, galactose oxidase, catalase, and horseradish peroxidase were co-immobilized into Cu3(PO4)2 nanoflowers in this study. The resulting co-immobilized tri-enzymes possessed better tolerance towards the oxidative damage caused by hydroxymethylfurfural at high concentrations, as compared to free tri-enzymes. Moreover, the 2,5-diformylfuran yield of co-immobilized tri-enzymes (95.7 ± 2.7%) was 1.06 times higher than that of separately immobilized enzymes (90.4 ± 1.9%). This result could be attributed to the boosted protective effect provided by catalase to the activity of galactose oxidase, owing to the physical proximity between them on the same support. After 30 recycles, co-immobilized tri-enzymes still achieves 86% of the initial yield. Moreover, co-immobilized tri-enzymes show enhanced thermal stability compared with free tri-enzymes. This work paves the way for the production of 2,5-diformylfuran from hydroxymethylfurfural via co-immobilized tri-enzymes.

show abstract

“…The temperature is an important parameter for the properties of enzymes [49,50,51,52]. The DFF yield was studied as a function of temperature ranging from 15–45 °C.…”

Section: Resultsmentioning

confidence: 99%

Co-Immobilization of Tri-Enzymes for the Conversion of Hydroxymethylfurfural to 2,5-Diformylfuran

Shi

et al. 2019

Molecules

View full text Add to dashboard Cite

show abstract

“… 53 The market value of food enzymes is estimated to exceed 3.6 billion US dollars by 2024, which justifies efforts in researching processes for obtaining, purifying, and stabilizing enzymes, which are the main concerns of industrial applications. 54 For an enzyme-mediated biotechnological process to be viable, it requires that these enzymes present high activity; high conversion rates; and stability at different temperatures, additives, and pH values. Recent advances in nanotechnology have made enzyme-mediated processes more profitable by providing stability, purification, and reuse facilities.…”

Section: Applications In Nanobiocatalysismentioning

confidence: 99%

“…Biocatalyzed processes by enzymes are preferred to chemicals, since they have advantages derived from their biological nature, process safety, high yield rates, and low environmental impact . The market value of food enzymes is estimated to exceed 3.6 billion US dollars by 2024, which justifies efforts in researching processes for obtaining, purifying, and stabilizing enzymes, which are the main concerns of industrial applications . For an enzyme-mediated biotechnological process to be viable, it requires that these enzymes present high activity; high conversion rates; and stability at different temperatures, additives, and pH values.…”

Section: Applications In Nanobiocatalysismentioning

confidence: 99%

“…These nanobiocatalysts have shown a higher selectivity for docosahexaenoic acid (DHA) and a similar degree of selectivity for eicosapentaenoic acid (EPA) when compared with the free enzyme. An efficiency of up to 95% of biocatalysis was optimized for a nanobiocatalyst obtained by covalent bonding and revealed excellent operational stability, and up to 20 reuse cycles could be achieved with only a loss of 50% of the biocatalytic potential; in addition, it presented a better thermochemical stability. , Another study for the hydrolysis of fish oil immobilized lipases from Thermomyces lanuginosus for the preparation of robust nanobiocatalysts using a carbon nanotube carrier. The authors demonstrated that higher enzyme loading, up to 6 mg enzyme per g of support, up to 1.6-fold higher DHA enrichment, with 80% operational stability after 6 reuses, was achieved …”

Section: Applications In Nanobiocatalysismentioning

confidence: 99%

See 1 more Smart Citation

Expanding the Scope of Nanobiocatalysis and Nanosensing: Applications of Nanomaterial Constructs

et al. 2022

View full text Add to dashboard Cite

The synergistic interaction between advanced biotechnology and nanotechnology has allowed the development of innovative nanomaterials. Those nanomaterials can conveniently act as supports for enzymes to be employed as nanobiocatalysts and nanosensing constructs. These systems generate a great capacity to improve the biocatalytic potential of enzymes by improving their stability, efficiency, and product yield, as well as facilitating their purification and reuse for various bioprocessing operating cycles. The different specific physicochemical characteristics and the supramolecular nature of the nanocarriers obtained from different economical and abundant sources have allowed the continuous development of functional nanostructures for different industries such as food and agriculture. The remarkable biotechnological potential of nanobiocatalysts and nanosensors has generated applied research and use in different areas such as biofuels, medical diagnosis, medical therapies, environmental bioremediation, and the food industry. The objective of this work is to present the different manufacturing strategies of nanomaterials with various advantages in biocatalysis and nanosensing of various compounds in the industry, providing great benefits to society and the environment.

show abstract

“…As a biocatalyst, lipase can not only hydrolyze triglycerides [ 15 , 16 ], but also catalyze the reverse synthesis of esters under certain conditions [ 17 , 18 ]. A previous study used the immobilized lipase Novozym ® 435 to esterify cinnamic acid with an alcohol in organic solvent media.…”

Section: Introductionmentioning

confidence: 99%

Ultrasound Plus Vacuum-System-Assisted Biocatalytic Synthesis of Octyl Cinnamate and Response Surface Methodology Optimization

Tsai

Huang

et al. 2022

Molecules

View full text Add to dashboard Cite

Cinnamic acid is one of the phenolic compounds that is isolated from cinnamon, or other natural plants, and has a wide range of physiological activities. However, the application of cinnamic acid is limited due to its poor solubility and low oral bioavailability. In this study, the feasibility of producing octyl cinnamate by ultrasonic assistance, combined with a rotary evaporation under vacuum, was studied using methyl cinnamate and octanol as the starting materials. A Box–Behnken design (BBD) was employed to evaluate the effects of the operation parameters, including reaction temperature (55–75 °C), reaction time (4–12 h), and ultrasonic power (90–150 W) on the production of octyl cinnamate. Meanwhile, the synthesis process was further optimized by the modeling response surface methodology (RSM). The data indicated that octyl cinnamate was efficiently synthesized from methyl cinnamate and octanol using the ultrasound plus vacuum system; further, this system was superior to the conventional method. According to the RSM model for the actual experiments, a reaction temperature of 74.6 °C, a reaction time of 11.1 h, and an ultrasound power of 150 W were determined to be the best conditions for the maximum molar conversion of octyl cinnamate (93.8%). In conclusion, the highly efficient synthesis of octyl cinnamate by a rotary evaporator with an ultrasound plus vacuum system was achieved via RSM optimization.

show abstract

Suitability of Recombinant Lipase Immobilised on Functionalised Magnetic Nanoparticles for Fish Oil Hydrolysis

Cited by 47 publications

References 42 publications

Co-Immobilization of Tri-Enzymes for the Conversion of Hydroxymethylfurfural to 2,5-Diformylfuran

Co-Immobilization of Tri-Enzymes for the Conversion of Hydroxymethylfurfural to 2,5-Diformylfuran

Expanding the Scope of Nanobiocatalysis and Nanosensing: Applications of Nanomaterial Constructs

Ultrasound Plus Vacuum-System-Assisted Biocatalytic Synthesis of Octyl Cinnamate and Response Surface Methodology Optimization

Contact Info

Product

Resources

About