Hydrolysis of oils by using immobilized lipase enzyme: A review

Murty, V. Ramachandra; Bhat, Jayashree S.; Muniswaran, P. K. A.

doi:10.1007/bf02935881

Cited by 180 publications

(95 citation statements)

References 25 publications

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“…In our study, E1, E2 and EE2 were degraded for the first time by Myceliophthora thermophila laccase immobilised on Eupergit C 250L support. However, the use of PBRs with immobilised enzymes could present some disadvantages such as: passive or poor aeration, slow mass transfer, the high pressure drop in the bed can provoke its compactation and hence biocatalyst damage, the possible formation of insoluble products which would lead to clogging phenomena, limitation in substrate's diffusion, intra particle diffusion limitations on reaction rates and possible leakage of the biocatalyst from the support (Gómez et al 2007;Murry et al 2002;O'Neill et al 1971;Osma et al 2010;Rekuc et al 2009). Additionally, long-term operation of packed bed reactor is still a challenge.…”

Section: Decolourisation Of a Model Synthetic Dye By Immobilised Laccasementioning

confidence: 99%

Immobilisation of laccase on Eupergit supports and its application for the removal of endocrine disrupting chemicals in a packed-bed reactor

et al. 2011

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Laccase from Myceliophthora thermophila was covalently immobilised on Eupergit C and Eupergit C 250L yielding specific activities of up to 17 and 80 U/g, respectively. Due to its superior activity, Eupergit C 250L was chosen for further research. The somewhat lower catalytic efficiency (based on the ratio between the turnover number and the Michaelis constant, k cat /K M ) of the immobilised enzyme in comparison with that of the free enzyme was balanced by its increased stability and broader operational window related to temperature and pH. The feasibility of the immobilised laccase was tested by using a packed bed reactor (PBR) operating in consecutive cycles for the removal of Acid Green 27 dye as model substrate. High degrees of elimination were achieved (88, 79, 69 and 57% in 4 consecutive cycles), while the levels of adsorption on the support varied from 18 to 6%, proving that dye removal took place mainly due to the action of the enzyme. Finally, a continuous PBR with the solid biocatalyst was applied for the treatment of a solution containing the following endocrine disrupting chemicals: estrone (E1), 17b-estradiol (E2) and 17a-ethinylestradiol (EE2). At steady-state operation, E1 was degraded by 65% and E2 and EE2 were removed up to 80% and only limited adsorption of these compounds on the support, between 12 and 22%, was detected. In addition, a 79% decrease in estrogenic activity was detected in the effluent of the enzymatic reactor while only 14% was attained by inactivated laccase.

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Section: Decolourisation Of a Model Synthetic Dye By Immobilised Laccasementioning

confidence: 99%

Immobilisation of laccase on Eupergit supports and its application for the removal of endocrine disrupting chemicals in a packed-bed reactor

et al. 2011

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“…Lipases (Triacylglycerol acylhydrolases, E.C. 3.1.1.3) are omnipresent enzymes of considerable industrial importance and physiological significance [6,7]. A considerable property of lipase(s) is the intense increase in lipase efficiency observed when the substrate starts to form an emulsion, by that means presenting to the enzyme an interfacial area [6,8].…”

Section: Introductionmentioning

confidence: 99%

Effect of Environmental and Nutritional Parameters on the Extracellular Lipase Production by <i>Aspergillus niger</i>

El-Batal

Farrag

Elsayed

et al. 2016

ILNS

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Abstract. The present investigation was carried out to evaluate the effect of different growth conditions on lipase production by Aspegillus niger. The extracellular lipase producing fungus was isolated from spent bleaching earths. Optimizations of physical and chemical parameters were done for maximum lipase production using this isolate. Growth of the organism and lipase production were measured usig varying pH (4 -9), incubation temperature (20 -30 °C), incubation time (8 -80 hrs.), carbon sources, nitrogen sources, and shaking speed. Enhanced lipase production was observed at 24 °C, pH 7 and after 72hrs of incubation. Olive oil 5 % was observed as the most effective carbon source and Yeast extract 1.0 % as the most effective nitrogen source for lipase production. The optimum shaking value to get maximum lipase activity by Aspergillus niger was 200 rpm.

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“…The immobilized enzyme bioreactor can be designed as stirred, packed, fluidized and membrane reactor that can be operated either in batch or continuous system [3]. Among these bioreactor, the stirred bioreactor is a most applied in bench scale and industrial scale application because it is versatile and easy to operate [4].…”

Section: Introductionmentioning

confidence: 99%

Effect of Agitation Speed for Enzymatic Hydrolysis of Tapioca Slurry Using Encapsulated Enzymes in an Enzyme Bioreactor

Rahim¹,

Sulaiman²,

Hamid³

et al. 2015

IJCEA

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Abstract-Agitation speed is an important factor in the industrial application for the mixing efficiency in order to increase productivity. In this study, the effect of agitation speed was investigated in a stirred bioreactor for hydrolysis of tapioca slurry into glucose by using encapsulated enzymes within calcium alginate-clay (alg-clay) beads. The hydrolysis process was tested at various agitation speeds from 40 to 200 rpm. The stability of alg-clay beads was examined in term of morphology of beads, enzyme leaching behavior and enzymes activity. The morphology of the alg-clay beads was investigated by Field Emission Scanning Electron Microscopy (FESEM). It was found that vigorous speed ruptured the beads structure. The result also showed that by increasing the agitation speed, the leakage of enzymes also increased. Therefore, it can be concluded that there was a strong correlation between the speed of agitation and the beads morphology. The optimum agitation speed which gave the highest amount of enzymes activity was 120 rpm.

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Hydrolysis of oils by using immobilized lipase enzyme: A review

Cited by 180 publications

References 25 publications

Immobilisation of laccase on Eupergit supports and its application for the removal of endocrine disrupting chemicals in a packed-bed reactor

Immobilisation of laccase on Eupergit supports and its application for the removal of endocrine disrupting chemicals in a packed-bed reactor

Effect of Environmental and Nutritional Parameters on the Extracellular Lipase Production by <i>Aspergillus niger</i>

Effect of Agitation Speed for Enzymatic Hydrolysis of Tapioca Slurry Using Encapsulated Enzymes in an Enzyme Bioreactor

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