scholarly journals Immobilization ofYarrowia lipolyticaLipase on Macroporous Resin Using Different Methods: Characterization of the Biocatalysts in Hydrolysis Reaction

2015 ◽  
Vol 2015 ◽  
pp. 1-7 ◽  
Author(s):  
Jingjing Sun ◽  
Yiling Chen ◽  
Jun Sheng ◽  
Mi Sun
Keyword(s):  
Immobilized Lipase ◽  
Solvent Tolerance ◽  
Alkaline Ph ◽  
Lipase Hydrolysis ◽  
Organic System ◽  
Microbial Lipase ◽  
Application Range ◽  
Immobilized Lipases ◽  
Free Lipase

To improve the reusability and organic solvent tolerance of microbial lipase and expand the application of lipase (hydrolysis, esterification, and transesterification), we immobilized marine microbial lipase using different methods and determined the properties of immobilized lipases. Considering the activity and cost of immobilized lipase, the concentration of lipase was fixed at 2 mg/mL. The optimal temperature of immobilized lipases was 40°C and 5°C higher than free lipase. The activities of immobilized lipases were much higher than free lipase at alkaline pH (more than 50% at pH 12). The free lipase lost most activity (35.3%) and immobilized lipases retained more than 46.4% of their initial activity after 3 h heat treatment at 70°C. At alkaline pH, immobilized lipases were more stable than free lipase (more than 60% residue activity at pH 11 for 3 h). Immobilized lipases retained 80% of their activity after 5 cycles and increased enzyme activity (more than 108.7%) after 3 h treatment in tert-butanol. Immobilization of lipase which improved reusability of lipase and provided a chance to expand the application of marine microbial lipase in organic system expanded the application range of lipase to catalyze hydrolysis and esterification in harsh condition.

scholarly journals Improved biodiesel from palm oil using lipase immobilized calcium alginate and Irvingia gabonensis matrices

2020 ◽  
Vol 9 (1) ◽  
Author(s):  
Sarafadeen Olateju Kareem ◽  
Esther Imole Falokun ◽  
Saka Adebayo Balogun ◽  
Oluwaseyi A. Akinloye ◽  
Sunday Osaizua Omeike
Keyword(s):  
Palm Oil ◽  
Calcium Alginate ◽  
Kinematic Viscosity ◽  
Immobilized Lipase ◽  
Flash Point ◽  
Fuel Properties ◽  
Biodiesel Production ◽  
Immobilized Lipases ◽  
Irvingia Gabonensis ◽  
Free Lipase

Abstract Background Lipase is an important microbial enzyme and biocatalyst in biodiesel production. The study investigated fuel properties of biodiesel produced from palm oil (PO) using lipase immobilized on Irvingia gabonensis and calcium alginate. Results Biodiesel yield from PO using free and immobilized lipases was highest at 35 °C and pH 7, with product yield using calcium alginate-immobilized lipase, CAIL (94.42, 96.9%) higher than using Irvingia gabonensis-immobilized lipase, IGIL (92.54, 95.8%). Biodiesel produced using immobilized lipases had similar pour point, cloud point, and kinematic viscosity, and they possessed improved fuel properties compared to free lipase biodiesel in terms of densities at 15 °C and flash point. Pour points, flash point, and kinematic viscosity of biodiesel produced using CAIL and IGIL met American and European Standards but density at 15 °C and cloud points are below both standards. CAIL and IGIL biodiesel had similar fatty acid methyl ester (FAME) compounds and consisted more of unsaturated fatty acids (hexadecanoate, 9-octadecenoate, octadecanoate, dodecanoate, and 9,12-octadeca-dienoate) than obtained in biodiesel from free lipase. IGIL and CAIL were re-used in 8 and 12 cycles respectively, with > 90% biodiesel yield achieved in four and 11 cycles. Conclusions The study showed that lipase immobilized on Irvingia gabenensis and calcium alginate and used in biodiesel production retained high enzyme activity and biodiesel yield in repeated cycles.

Partial purification and characterization of free and immobilized lipases fromMucor miehei

Lipids ◽  
1987 ◽  
Vol 22 (9) ◽  
pp. 680-680
Author(s):  
Birgitte Huge-Jensen ◽  
Donna Rubano Galluzzo ◽  
Robert G. Jensen
Keyword(s):  
Partial Purification ◽  
Purification And Characterization ◽  
Immobilized Lipases

scholarly journals Immobilization of Isolated Lipase From Moldy Copra(Aspergillus Oryzae)

2011 ◽  
Vol 8 (2) ◽  
pp. 896-902
Author(s):  
Seniwati Dali ◽  
A. B. D. Rauf Patong ◽  
M. Noor Jalaluddin ◽  
Pirman ◽  
Baharuddin Hamzah
Keyword(s):  
Thermal Stability ◽  
Aspergillus Oryzae ◽  
Immobilized Lipase ◽  
Optimum Temperature ◽  
Adsorption Method ◽  
Ph Optimum ◽  
Optimum Ph ◽  
Recovery Technique ◽  
Free Lipase

Enzyme immobilization is a recovery technique that has been studied in several years, using support as a media to help enzyme dissolutions to the reaction substrate. Immobilization method used in this study was adsorption method, using specific lipase fromAspergillus oryzae. Lipase was partially purified from the culture supernatant ofAspergillus oryzae. Enzyme was immobilized by adsorbed on silica gel. Studies on free and immobilized lipase systems for determination of optimum pH, optimum temperature, thermal stability and reusability were carried out. The results showed that free lipase had optimum pH 8,2 and optimum temperature 35 °C while the immobilized lipase had optimum 8,2 and optimum temperature 45 °C. The thermal stability of the immobilized lipase, relative to that of the free lipase, was markedly increased. The immobilized lipase can be reused for at least six times.

CONSTRUCTION AND CHARACTERIZATION OF A NANOSTRUCTURED BIOCATALYST CONSISTING OF IMMOBILIZED LIPASE ON Mg-AMINO-CLAY

2021 ◽  
Author(s):  
Mingzhu Zhang ◽  
Shiyong Sun ◽  
Rui Lv ◽  
Yevgeny Aleksandrovich Golubev ◽  
Ke Wang ◽  
...  
Keyword(s):  
Immobilized Lipase

scholarly journals ISOLATION, PURIFICATION, AND CHARACTERIZATION OF LIPASE FROM BACILLUS SP. FROM KITCHEN GREASE

2018 ◽  
Vol 11 (6) ◽  
pp. 224
Author(s):  
Jaiganesh R ◽  
Jaganathan Mk
Keyword(s):  
16S Rdna ◽  
Solvent Tolerance ◽  
16S Rdna Sequencing ◽  
Bacillus Sp ◽  
Purification And Characterization ◽  
Lipase Enzyme ◽  
Sequencing Method ◽  
Rdna Sequencing ◽  
Solvent Tolerant

Objective: The objective of this work was to isolation, purification and characterization of solvent tolerant lipase from Bacillus sp. The objective of this work was to isolation, purification and characterization of solvent tolerant lipase from Bacillus sp. from kitchen grease for a variety of applications including organic synthetic reactions and preparation of enantiomerically pure pharmaceuticals.Methods: Lipase producing isolates were screened from kitchen grease on a selective medium rhodamine B olive oil agar, and tributyrin agar was used to screen the lipase and esterase producing an organism, respectively. The isolate identified using 16S rDNA sequencing method and enzyme activity was quantitatively assayed. Lipase production was characterized in different conditions.Results: The isolate showed highest lipase activity was which later was identified as Bacillus sp. using 16S rDNA sequencing method. The lipase was purified using ammonium sulfate precipitation. The isolate showed excellent tolerance to methanol, ethanol, acetonitrile, and moderate tolerance to butanol. The increased biomass concentration, maximum production, and activity were achieved at 37°C in 24 h incubation, then gradual reduction in production was observed. The maximum activity of lipase enzyme was obtained at pH between 6 and 9.Conclusion: The isolate produce solvent tolerance lipase enzyme and it can be a promising candidate of solvent tolerance lipase enzyme for variety of industrial applications.

scholarly journals Screening and Comparative Characterization of Microorganisms from Iranian Soil Samples Showing ω-Transaminase Activity toward a Plethora of Substrates

Catalysts ◽  
2019 ◽  
Vol 9 (10) ◽  
pp. 874 ◽  
Author(s):  
Najme Gord Noshahri ◽  
Jamshid Fooladi ◽  
Christoph Syldatk ◽  
Ulrike Engel ◽  
Majid M. Heravi ◽  
...  
Keyword(s):  
Soil Microorganisms ◽  
Solvent Tolerance ◽  
Chiral Amines ◽  
Optimal Conditions ◽  
Transaminase Activity ◽  
Rdna Sequencing ◽  
High Enzyme ◽  
Amino Donor ◽  
Selection Of

In this study, soil microorganisms from Iran were screened for ω-transaminase (ω-TA) activity based on growth on minimal media containing (rac)-α-methylbenzylamine (rac-α-MBA) as a sole nitrogen source. Then, for the selection of strains with high enzyme activity, a colorimetric o-xylylendiamine assay was conducted. The most promising strains were identified by 16S rDNA sequencing. Five microorganisms showing high ω-TA activity were subjected to determine optimal conditions for ω-TA activity, including pH, temperature, co-solvent, and the specificity of the ω-TA toward different amine donors and acceptors. Among the five screened microorganisms, Bacillus halotolerans turned out to be the most promising strain: Its cell-free extract showed a highly versatile amino donor spectrum toward aliphatic, aromatic chiral amines and a broad range of pH activity. Transaminase activity also exhibited excellent solvent tolerance, with maximum turnover in the presence of 30% (v/v) DMSO.

scholarly journals Lipase NS81006 immobilized on Fe3O4 magnetic nanoparticles for biodiesel production

2016 ◽  
Vol 27 (1) ◽  
pp. 13-21 ◽  
Author(s):  
Baskar Thangaraj ◽  
Zhaohua Jia ◽  
Lingmei Dai ◽  
Dehua Liu ◽  
Wei Du
Keyword(s):  
Magnetic Nanoparticles ◽  
Immobilized Lipase ◽  
Biodiesel Production ◽  
Molar Ratio ◽  
Fe3o4 Magnetic Nanoparticles ◽  
Time Duration ◽  
Fast Reaction ◽  
Functionalized Magnetic Nanoparticles ◽  
Optimized Conditions ◽  
Free Lipase

Abstract Lipase-catalyzed biodiesel production is being the object of extensive research due to the demerits of chemical based catalytic system. Lipase immobilized on Fe3O4 magnetic nanoparticles has the integrated advantages of traditional immobilized lipase and free lipase for its rather fast reaction rate and easy separation. It has been demonstrated that free lipase NS81006 has potential in catalyzing the alcoholysis of renewable oils for biodiesel preparation. In this study, Fe3O4 magnetic nanoparticles functionalized with organosilane compounds like (3-aminopropyl)triethyloxysilane (APTES) and (3-mercaptopropyl)trimethoxysilane) MPTMS were used as carriers for lipase immobilization. Lipase NS81006 was covalently bound to the organosilane-functionalized magnetic nanoparticles by using glutaraldehyde cross-linking reagent. A biodiesel yield of 89% and 81% could be achieved by lipase immobilized on APTES-Fe3O4 and MPTMS-Fe3O4 magnetic nanoparticles respectively under optimized conditions of oil to methanol molar ratio 1:3 with three step addition of methanol, reaction temperature 45°C and reaction time duration 12 h. The lipases immobilized on magnetic nanoparticles could be recovered easily by external magnetic field for further use.

scholarly journals Characterization of the Novel Ene Reductase Ppo-Er1 from Paenibacillus Polymyxa

Catalysts ◽  
2020 ◽  
Vol 10 (2) ◽  
pp. 254 ◽  
Author(s):  
David Aregger ◽  
Christin Peters ◽  
Rebecca M. Buller
Keyword(s):  
Enantiomeric Excess ◽  
Asymmetric Hydrogenation ◽  
Paenibacillus Polymyxa ◽  
Solvent Tolerance ◽  
Old Yellow Enzyme ◽  
Conversion Rates ◽  
Specificity Constant ◽  
Km Value ◽  
Ph Range

Ene reductases enable the asymmetric hydrogenation of activated alkenes allowing the manufacture of valuable chiral products. The enzymes complement existing metal- and organocatalytic approaches for the stereoselective reduction of activated C=C double bonds, and efforts to expand the biocatalytic toolbox with additional ene reductases are of high academic and industrial interest. Here, we present the characterization of a novel ene reductase from Paenibacillus polymyxa, named Ppo-Er1, belonging to the recently identified subgroup III of the old yellow enzyme family. The determination of substrate scope, solvent stability, temperature, and pH range of Ppo-Er1 is one of the first examples of a detailed biophysical characterization of a subgroup III enzyme. Notably, Ppo-Er1 possesses a wide temperature optimum (Topt: 20–45 °C) and retains high conversion rates of at least 70% even at 10 °C reaction temperature making it an interesting biocatalyst for the conversion of temperature-labile substrates. When assaying a set of different organic solvents to determine Ppo-Er1′s solvent tolerance, the ene reductase exhibited good performance in up to 40% cyclohexane as well as 20 vol% DMSO and ethanol. In summary, Ppo-Er1 exhibited activity for thirteen out of the nineteen investigated compounds, for ten of which Michaelis–Menten kinetics could be determined. The enzyme exhibited the highest specificity constant for maleimide with a kcat/KM value of 287 mM−1 s−1. In addition, Ppo-Er1 proved to be highly enantioselective for selected substrates with measured enantiomeric excess values of 92% or higher for 2-methyl-2-cyclohexenone, citral, and carvone.

Characterization of pre-gelatinized maize starch-zein blend films produced at alkaline pH

2020 ◽  
Vol 95 ◽  
pp. 103083
Author(s):  
Welday Hailu Teklehaimanot ◽  
Suprakas Sinha Ray ◽  
M. Naushad Emmambux
Keyword(s):  
Alkaline Ph ◽  
Maize Starch ◽  
Blend Films
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