Kinetic and docking study of synthesis of glyceryl monostearate by immobilized lipase in non-aqueous media

Author(s):  
Priyanka V. Jawale ◽  
Bhalchandra M. Bhanage
Nanomaterials ◽  
2019 ◽  
Vol 9 (6) ◽  
pp. 808 ◽  
Author(s):  
Renia Fotiadou ◽  
Michaela Patila ◽  
Mohamed Amen Hammami ◽  
Apostolos Enotiadis ◽  
Dimitrios Moschovas ◽  
...  

In the present study, hybrid nanoflowers (HNFs) based on copper (II) or manganese (II) ions were prepared by a simple method and used as nanosupports for the development of effective nanobiocatalysts through the immobilization of lipase B from Pseudozyma antarctica. The hybrid nanobiocatalysts were characterized by various techniques including scanning electron microscopy (SEM), energy dispersion spectroscopy (EDS), X-ray diffraction (XRD), Raman spectroscopy, and Fourier transform infrared spectroscopy (FTIR). The effect of the addition of carbon-based nanomaterials, namely graphene oxide and carbon nanotubes, as well as magnetic nanoparticles such as maghemite, on the structure, catalytic activity, and operational stability of the hybrid nanobiocatalysts was also investigated. In all cases, the addition of nanomaterials during the preparation of HNFs increased the catalytic activity and the operational stability of the immobilized biocatalyst. Lipase-based magnetic nanoflowers were effectively applied for the synthesis of tyrosol esters in non-aqueous media, such as organic solvents, ionic liquids, and environmental friendly deep eutectic solvents. In such media, the immobilized lipase preserved almost 100% of its initial activity after eight successive catalytic cycles, indicating that these hybrid magnetic nanoflowers can be applied for the development of efficient nanobiocatalytic systems.


2016 ◽  
Vol 84 ◽  
pp. 1-10 ◽  
Author(s):  
Ashwini C. Mathpati ◽  
Kirtikumar C. Badgujar ◽  
Bhalchandra M. Bhanage

2016 ◽  
Vol 18 (3) ◽  
pp. 134-140 ◽  
Author(s):  
Cansu Ulker ◽  
Nurefsan Gokalp ◽  
Yuksel Guvenilir

Abstract In the present study, rice husk ash, which is a renewable and abundant material, was utilized as a carrier for lipase immobilization for the first time. Poly (ε-caprolactone) synthesis was successfully achieved by the new enzymatic catalyst: Candida antarctica lipase B immobilized onto surface-modified rice husk ashes by covalent binding. It was aimed to obtain optimum polymerization conditions at which highest molecular weight was reached and characterize the polymer produced. Moreover, thermal stability and effectiveness of the new biocatalyst in non-aqueous media were also shown with successful polymerization reactions. In addition, by using the new enzyme preparation, ε-caprolactone was able to be polymerized even at 30°C, which was promising for an energy saving process. Consequently, this work provides a new alternative route for poly (ε-caprolactone) synthesis.


2019 ◽  
Vol 278 ◽  
pp. 536-545 ◽  
Author(s):  
Jagannath Panda ◽  
Jitendra Kumar Sahoo ◽  
Prasanna Kumar Panda ◽  
Satya Narayan Sahu ◽  
Mahalaxmi Samal ◽  
...  

2016 ◽  
Vol 14 (4) ◽  
pp. 919-928 ◽  
Author(s):  
Moreshwar P. Hude ◽  
Janusz Kozinski ◽  
Ajay K. Dalai ◽  
Ganapati D. Yadav

Abstract Hexagonal mesoporous type silica SBA-15 with pore sizes in the range 5.0–8.3 nm was synthesized using non-ionic triblock copolymer and characterized by Accelerated Surface Area Porosimetry (ASAP), FT-IR spectroscopy, X-ray diffraction (XRD) and Scanning Electron Microscopy (SEM). Different lipases were immobilized in glutaraldehyde activated mesoporous SBA-15 support. The resulting supported enzymes were shown to be active and stable catalysts for esterification of glycerol with oleic acid to produce monoglyceride (MG) which is commonly used in food industry. Various parameters were studied systematically to study kinetics. MG Synthesis using enzymatic process is an environmentally friendly approach. Enzyme immobilized on SBA-15 showed the best stability and catalytic activity in organic solvents. Out of various lipases studied penicillium camembertii (Lipase G) produced MG efficiently at low temperature. Reusability was studied on immobilized enzymes. Immobilized lipase maintained 90 % of its esterification activity in non-aqueous media even after 4 cycles of use. The selectivity of Lipase G is found to be 98 % for monoacylglyceride.


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