Isoamylacetate production by entrapped and covalently bound Candida rugosa and porcine pancreatic lipases

Özyılmaz, Gül; Yağız, Esra

doi:10.1016/j.foodchem.2012.07.062

Cited by 26 publications

(27 citation statements)

References 31 publications

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“…1,2 Different immobilization techniques are present using various support materials and methods. [3][4][5] Among these, entrapment is very straightforward for biocatalyst immobilization under moderate conditions relative to other immobilization techniques. 6 Calcium alginate beads are one of the most frequently used carriers in the immobilization of enzymes by entrapment because they have some advantages including cost-effective, favorable biocompatibility, high stability against microbial attack, and availability.…”

Section: Introductionmentioning

confidence: 99%

Thermoalkalophilic recombinant esterase entrapment in chitosan/calcium/alginate‐blended beads and its characterization

Tercan

Sürmeli

Şanlı‐Mohamed

2021

J of Chemical Tech & Biotech

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BACKGROUND: Esterases (EC 3.1.1.1), a class of hydrolases, degrade the ester bonds of lipids into alcohol and carboxylic acids and synthesize carboxylic ester bonds. They are used in a variety of biotechnological, industrial, environmental, and pharmaceutical applications due to their many valuable properties. Particularly, extremophilic esterases with many superior properties are of great interest for various reactions. Immobilization of enzymes may provide some advantages over free enzymes not only to improve the properties of enzymes but also to increase the reusability of biocatalyst in industrial applications. Therefore, many different immobilization applications for enzymes have been reported in various studies. To our knowledge, a thermophilic esterase has not so far been immobilized by entrapment using chitosan/calcium/alginate-blended beads. Here, we reported the immobilization of thermoalkalophilic recombinant esterase by entrapment using chitosan/calcium/alginateblended beads, and then the entrapped esterase was characterized biochemically in details.RESULTS: In the present study, a thermophilic recombinant esterase was immobilized by entrapment in chitosan/calcium/alginateblended beads for the first time. The 0.5 mg mL −1 purified recombinant esterase was entrapped in 1% chitosan, 2% alginate, and 0.7 M CaCl 2 blended beads. The results showed that immobilization yield and entrapment efficiency of the entrapped esterase were 69.5% and 80.4%, respectively. SEM micrograph showed that the surface of the beads resembled a mesh and very compact structures. Chitosan/calcium/alginate-blended beads exhibited an 18.8% swelling ratio and had a moderate porous structure. The entrapment technique highly enhanced the thermostability of the esterase and shifted its optimum temperature from 65 to 80°C. The immobilized esterase was very stable in a wide range of pH (8.5-11) displaying maximum activity at pH 9. ZnCl 2 slightly increased the activity of immobilized esterase whereas several metal ions reduced the enzyme activity. When the enzyme was immobilized in chitosan/calcium/alginate-blended beads, its K m increased about 2 times and V max value decreased almost 1.5 times. Immobilization allowed repeated uses of the esterase having good operational stability in a continuous process. CONCLUSION:The results revealed that the immobilization of a thermophilic recombinant esterase by entrapment in chitosan/ calcium/alginate-blended beads exhibited considerably better compared to other immobilization processes with various entrapment strategies.

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Section: Introductionmentioning

confidence: 99%

Thermoalkalophilic recombinant esterase entrapment in chitosan/calcium/alginate‐blended beads and its characterization

Tercan

Sürmeli

Şanlı‐Mohamed

2021

J of Chemical Tech & Biotech

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“…Esters can also be obtained from higher alcohols of fuel oil, which are used as solvents, flavoring agents, medicinal, and plasticizers [48]. Isoamyl esters (such as isoamyl acetate) are aromatic compounds that are widely used in the food and beverage industry (because they have important compounds of flavor and fragrance) [49]. Other aromatic compounds produced by yeasts, such as acetates, also show commercial applications and have been used as components in flavorings (ethyl acetate, isobutyl acetate, amyl acetates, and isoamyl acetate) and additives for perfume (isopropyl acetates, acetates of octyl, and methyl acetates).…”

Section: Higher Alcohols and Aromatic Compounds Production From S Cementioning

confidence: 99%

Comparative of Lignocellulosic Ethanol Production by Kluyveromyces marxianus and Saccharomyces cerevisiae

Amaya-Delgado¹,

Flores-Cosío²,

Nuñez³

et al. 2018

Special Topics in Renewable Energy Systems

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The world faces a progressive depletion of its energy resources, mainly fossil fuels based on non-renewable resources. At the same time, the consumption of energy grows at high rates, and the intensive use of fossil fuels has led to an increase in the generation of gaseous pollutants released into the atmosphere, which has caused changes in the global climate. The lignocellulosic bioethanol is considered as a promising alternative for use as fuel ethanol. However, one of the main problems in producing ethanol is toxic compounds generated during hydrolysis of lignocellulosic wastes; these compounds cause a longer lag phase and irreversible cell damage to the microorganisms used in the fermentation step. These conditions of fermentation affect the productivity and the economic feasibility of the lignocellulosic ethanol production process. In this context, many efforts had been carried out to improve the capacity of volumetric ethanol productivity of the yeast. The yeast Saccharomyces cerevisiae is commonly employed in industrial ethanol production. However non-Saccharomyces yeast as Kluyveromyces marxianus can produce alcohols at similar or higher levels than S. cerevisiae and on inhibitory conditions.

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“…Various physical and chemical immobilization techniques have been reported using diverse support materials [4]. Recently, among these techniques, the immobilization of the biocatalysts onto magnetic nanoparticles (MNPs) has been extensively applied because of their advantageous properties [5][6][7].…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Thermoalkalophilic Esterase Onto Magnetic-Cornstarch Nanoparticle

Öz

Sürmeli

Şanlı‐Mohamed

2021

Preprint

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The immobilization of the biocatalysts onto magnetic nanoparticles (MNPs) has been extensively applied since the external magnetic field facilitates the enzyme recovery from the reaction mixture. In the present study, glutaraldehyde-modified magnetite-cornstarch nanoparticles (MCNs) were successfully synthesized, elaborately characterized by ZetaSizer and surface-enhanced raman spectroscopy (SERS), and used for the immobilization of a thermoalkalophilic esterase from Geobacillus sp. The optimal immobilization conditions were obtained at 65oC, 2:3 molar ratios of Fe2+:Fe3+ and 1 g cornstarch resulted in approximately 90 nm magnetic particles in size. Also, immobilization yield and entrapment efficiency of the esterase were found as 74% and 82%, respectively. Scanning Electron Microscopy (SEM) micrographs showed that MCNs were uniform, spherical in shape, and well dispersed and esterase immobilized MCNs displayed similar morphology as free MCNs. The maximum activity of free and immobilized esterase was obtained at 80oC and pH 9. Immobilization onto glutaraldehyde-modified MCNs significantly enhanced the esterase thermostability. Additionally, the immobilized esterase kept its residual activity of 75% after three sequential cycles, suggesting that it has favorable operational stability.

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Isoamylacetate production by entrapped and covalently bound Candida rugosa and porcine pancreatic lipases

Cited by 26 publications

References 31 publications

Thermoalkalophilic recombinant esterase entrapment in chitosan/calcium/alginate‐blended beads and its characterization

Thermoalkalophilic recombinant esterase entrapment in chitosan/calcium/alginate‐blended beads and its characterization

Comparative of Lignocellulosic Ethanol Production by Kluyveromyces marxianus and Saccharomyces cerevisiae

Immobilization of Thermoalkalophilic Esterase Onto Magnetic-Cornstarch Nanoparticle

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