Immobilization of Candida rugosa lipase on MSU-H type mesoporous silica for selective esterification of conjugated linoleic acid isomers with ethanol

Yu, Wei; Tong, Dong Shen; Fang, Mei; Shao, Ping; Zhou, Chun Hui

doi:10.1016/j.molcatb.2014.11.003

Cited by 25 publications

(11 citation statements)

References 56 publications

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“…Since the immobilization process takes place by covalent bonding between primary amino groups on the side chain of lipase and free aldehyde groups on the support [28,41], the observed decrease in activity of the immobilized lipase beyond 40 mg/L initial enzyme concentrations could be due to difficulty in assuming their active conformations when excessive amounts of enzyme molecules were immobilized or it could be due to problems with the diffusion of the substrate or the aggregation of the enzyme in solutions. Similar results were also observed by Gunha et al and Yu et al [43,44].…”

Section: Effect Of Initial Concentration Of Lipase Solutionsupporting

confidence: 91%

Collagen-Immobilized Lipases Show Good Activity and Reusability for Butyl Butyrate Synthesis

Song

Chen

Cheng

2016

Appl Biochem Biotechnol

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Candida rugosa lipases were immobilized onto collagen fibers through glutaraldehyde cross-linking method. The immobilization process has been optimized. Under the optimal immobilization conditions, the activity of the collagen-immobilized lipase reached 340 U/g. The activity was recovered of 28.3 % by immobilization. The operational stability of the obtained collagen-immobilized lipase for hydrolysis of olive oil emulsion was determined. The collagen-immobilized lipase showed good tolerance to temperature and pH variations in comparison to free lipase. The collagen-immobilized lipase was also applied as biocatalyst for synthesis of butyl butyrate from butyric acid and 1-butanol in n-hexane. The conversion yield was 94 % at the optimal conditions. Of its initial activity, 64 % was retained after 5 cycles for synthesizing butyl butyrate in n-hexane.

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Section: Effect Of Initial Concentration Of Lipase Solutionsupporting

confidence: 91%

Collagen-Immobilized Lipases Show Good Activity and Reusability for Butyl Butyrate Synthesis

Song

Chen

Cheng

2016

Appl Biochem Biotechnol

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“…When lipase concentrations were higher than 30 mg/mL, the observed activity of MNp-Col-IL was lower, indicating that excessive immobilized enzymes on the support could hamper their transformation into active conformations for catalysis of the hydrolysis reaction. Similar results were observed by others [21,24]. Furthermore, the immobilization procedure may cause secondary structural changes to the enzyme molecules, especially when some multipoint covalent bonds are built between the support and the enzyme [25].…”

Section: Initial Concentration Of Lipase Solutionsupporting

confidence: 86%

Immobilization of Lipases on Magnetic Collagen Fibers and Its Applications for Short-Chain Ester Synthesis

Song

Chen

et al. 2017

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Magnetic nanoparticles (MNp) Fe 3 O 4 were prepared by chemical coprecipitation, and introduced onto collagen fibers to form magnetic collagen support (MNp-Col) for enzyme immobilization. Candida rugosa lipase has been successfully immobilized on MNp-Col supports by a covalent bond cross-linking agent, glutaraldehyde. The characteristics of MNp-Col and the immobilized lipase were investigated. The immobilized lipase displayed sound magnetic separation abilities in both aqueous and organic media. The activity of the immobilized lipase reached 2390 U/g under optimal conditions. The MNp-Col immobilized lipase shows broadened temperature and pH ranges for hydrolysis of olive oil emulsion. For synthesis of butyrate esters in an n-hexane medium, the yield changes through use of different alcohols, among which, butyric butyrate showed the highest yield. The prepared magnetic collagen fiber provides separation support for enzyme immobilization and has the potential to be used in other biotechnology fields.

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“…However, the most commonly used inorganic support for lipase, as well as other enzyme immobilization is silica [26][27][28][29]. A lipase immobilized on magnesium silicate hydrate (MSH) has been used for selective esterification of conjugated linoleic acid isomers with ethanol [30]. Another type of silica, SBA-15, was modified by ionic liquids and used for lipase immobilization [31].…”

Section: Introductionmentioning

confidence: 99%

Lipase B from Candida antarctica Immobilized on a Silica-Lignin Matrix as a Stable and Reusable Biocatalytic System

et al. 2016

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A study was conducted of the possible use of a silica-lignin hybrid as a novel support for the immobilization of lipase B from Candida antarctica. Results obtained by elemental analysis, Fourier transform infrared spectroscopy (FTIR), X-ray photoelectron spectroscopy (XPS), and atomic force microscopy (AFM), as well as the determination of changes in porous structure parameters, confirmed the effective immobilization of the enzyme on the surface of the composite matrix. Based on a hydrolysis reaction, a determination was made of the retention of activity of the immobilized lipase, found to be 92% of that of the native enzyme. Immobilization on a silica-lignin matrix produces systems with maximum activity at pH = 8 and at a temperature of 40 • C. The immobilized enzyme exhibited increased thermal and chemical stability and retained more than 80% of its activity after 20 reaction cycles. Moreover immobilized lipase exhibited over 80% of its activity at pH range 7-9 and temperature from 30 • C to 60 • C, while native Candida antarctica lipase B (CALB) exhibited the same only at pH = 7 and temperature of 30 • C.

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Immobilization of Candida rugosa lipase on MSU-H type mesoporous silica for selective esterification of conjugated linoleic acid isomers with ethanol

Cited by 25 publications

References 56 publications

Collagen-Immobilized Lipases Show Good Activity and Reusability for Butyl Butyrate Synthesis

Collagen-Immobilized Lipases Show Good Activity and Reusability for Butyl Butyrate Synthesis

Immobilization of Lipases on Magnetic Collagen Fibers and Its Applications for Short-Chain Ester Synthesis

Lipase B from Candida antarctica Immobilized on a Silica-Lignin Matrix as a Stable and Reusable Biocatalytic System

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