Solvent-Free Synthesis of Flavour Esters through Immobilized Lipase Mediated Transesterification

Garlapati, Vijay Kumar; Banerjee, Rintu

doi:10.1155/2013/367410

Cited by 55 publications

(30 citation statements)

References 34 publications

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“…After 3 cycles, the activity remained about 50% of the initial activity. Similar results were shown by [15,37,38]. The acid values of this study were relatively low compared to literature which uses commercial immobilized lipase with a remaining activity of 50% after 5 times cycles.…”

Section: Reusability Studiessupporting

confidence: 85%

A Performance Study of Home-Made Co-Immobilized Lipase from Mucor miehei in Polyurethane Foam on The Hydrolysis of Coconut Oil to Fatty Acid

Moentamaria

Muharja

Widjaja

et al. 2019

Bull. Chem. React. Eng. Catal.

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Bio-based fatty acids (FAs) produced through hydrolysis of natural oils and fats are promising chemical feedstocks for increasing the economic value of renewable raw materials. In this work, lecithin, gelatin, PEG, and MgCl2 were employed as the co-immobilized material of crude lipase Mucor miehei immobilization on the polyurethane foam (PUF) matrix for hydrolysis of coconut oil to Free Fatty Acid (FFA). The unconventional immobilized technique was used through cross-linking and covalent bond. Single factor analysis and response surface method were utilized to determine the optimum conditions of the hydrolysis reaction. After optimization, co-immobilized lipase was examined for storage stability at a temperature of 4°C and reusability performance. The optimum conditions for coconut oil hydrolysis were obtained on the co-immobilized-PUF ratio, water-oil ratio, and reaction time of 20.17 w/w, 4.45 w/w, and 20 h, respectively. Under these conditions, the acid value as lauric acid enhanced 573% to 3.21 mg KOH/g oil. Storage stability attained through remaining activity on free lipase, PUF-lipase, PUF-co-immobilized-lipase were 9.89%, 42.3%, and 91.88%, respectively. In this study, the application of PUF-co-immobilized lipase in hydrolysis reactions can be reused up to 5 times. Characteristics of the addition of co-immobilized lipase have been analyzed using Fourier Transform Infra Red (FTIR) and Scanning Electron Microscope (SEM), showing the presence of functional groups binding and the changes in the surface matrix structure.

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Section: Reusability Studiessupporting

confidence: 85%

A Performance Study of Home-Made Co-Immobilized Lipase from Mucor miehei in Polyurethane Foam on The Hydrolysis of Coconut Oil to Fatty Acid

Moentamaria

Muharja

Widjaja

et al. 2019

Bull. Chem. React. Eng. Catal.

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“…Conversely, in non-aqueous media, lipases can use other nucleophiles, such as methanol, to catalyse esterification and transesterification reactions [2][3][4][5][6][7][8][9][10][11][12][13] , although the explicit removal of water is not often a priority. Typically, enzyme reactions performed in organic solvents still contain a hydration layer at the surface of the protein, and the pervasiveness of the solvent in these examples highlights the requirement for a substrate delivery medium [14][15][16][17][18][19][20][21][22][23][24][25] .…”

mentioning

confidence: 99%

“…Typically, enzyme reactions performed in organic solvents still contain a hydration layer at the surface of the protein, and the pervasiveness of the solvent in these examples highlights the requirement for a substrate delivery medium [14][15][16][17][18][19][20][21][22][23][24][25] . There have also been reports of lipase catalysis where the reaction proceeds with solvent quantities of one of the reagents 3,12,13 , where the lipases are typically present as either a lyophilized powder 12,13,26 , or immobilized on a substrate 2,3,8,10,27,28 , but there are no examples of molecularly dispersed enzymes catalysing reactions in the complete absence of a solvent.…”

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confidence: 99%

Enzyme activity in liquid lipase melts as a step towards solvent-free biology at 150 °C

et al. 2014

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Water molecules play a number of critical roles in enzyme catalysis, including mass transfer of substrates and products, nucleophilicity and proton transfer at the active site, and solvent shell-mediated dynamics for accessing catalytically competent conformations. The pervasiveness of water in enzymolysis therefore raises the question concerning whether biocatalysis can be undertaken in the absence of a protein hydration shell. Lipase-mediated catalysis has been undertaken with reagent-based solvents and lyophilized powders, but there are no examples of molecularly dispersed enzymes that catalyse reactions at sub-solvation levels within solvent-free melts. Here we describe the synthesis, properties and enzyme activity of self-contained reactive biofluids based on solvent-free melts of lipase-polymer surfactant nanoconjugates. Desiccated substrates in liquid (p-nitrophenyl butyrate) or solid (p-nitrophenyl palmitate) form can be mixed or solubilized, respectively, into the enzyme biofluids, and hydrolysed in the solvent-free state. Significantly, the efficiency of product formation increases as the temperature is raised to 150°C.

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“…Nonaqueous systems (organic solvents such as n-hexane) were examined to improve the ester yield and to simplify the isolation and purification steps. Also immobilized lipase mediated transesterification was tired to produce flavor esters (Garlapati and Banerjee, 2013).…”

Section: Estersmentioning

confidence: 99%

Other Organism‐Based Processes and Products

Lee

2014

Fundamentals of Food Biotechnology

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Enzymes, which are protein catalysts synthesized by living systems, are important as synthetic and degradative catalysts. With the help of a multitude of enzymes, microorganisms are able to carry out the huge number of stepwise chemical reactions necessary for the growth and maintenance of cells (metabolism). Many microorganisms synthesize additional, often complex substances, which play no part in the growth process, the so-called secondary metabolites such as flavor and fragrances. Most of the chemical reactions taking place in living cells are completed in milliseconds or less, within a relatively narrow range of physical conditions. This rapid rate of metabolism is due to the existence of biological catalysts, namely enzymes. Enzymes not only make essential contributions to cellular activities, but also find many applications in biotechnology, especially in the food processing industry, for manufacturing cheese, beer, wine, bread, sweeteners, and so on, and in the chemical and pharmaceutical industries for synthesizing amino acids and antibiotics.While the presence of natural enzymes is advantageous in curing food products such as cheese and meat to give desirable textures and flavors, natural enzymes may produce undesirable reactions, such as rancidity from lipases and browning reactions due to polyphenol oxidases. Sometimes natural enzymes in foods are used as an index of the pasteurization of milk or cheese (by the detection of phosphatase or catalase) or to indicate the presence of peroxidase in vegetable products (as evidence of incomplete blanching). Recognition of the functions and the usefulness of enzymes in bringing about desirable changes in foods has led to the large-scale production of commercial enzymes. Of the more than 4000 enzymes known from animal, plant, or microbial sources, fewer than 20 are industrially produced on a large scale for the production of foods and intermediates. The majority of enzymes are hydrolases such as amylases, cellulases, pectinases, and proteases, which degrade polymeric substances to simple molecules. The world market for total enzymes is predicted to $7 billion in 2013

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Solvent-Free Synthesis of Flavour Esters through Immobilized Lipase Mediated Transesterification

Cited by 55 publications

References 34 publications

A Performance Study of Home-Made Co-Immobilized Lipase from Mucor miehei in Polyurethane Foam on The Hydrolysis of Coconut Oil to Fatty Acid

A Performance Study of Home-Made Co-Immobilized Lipase from Mucor miehei in Polyurethane Foam on The Hydrolysis of Coconut Oil to Fatty Acid

Enzyme activity in liquid lipase melts as a step towards solvent-free biology at 150 °C

Other Organism‐Based Processes and Products

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