Hydrolysis of triacetin catalyzed by immobilized lipases: Effect of the immobilization protocol and experimental conditions on diacetin yield

Hernández, Karel; García‐Verdugo, Eduardo; Porcar, Raúl; Fernández‐Lafuente, Roberto

doi:10.1016/j.enzmictec.2011.02.005

Cited by 53 publications

(41 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Retention times were 25 min for triacetin and 5 min for diacetin. Activity was determined with a maximum conversion of 15–20%, as at pH 7 there are acyl migration and 1,3 diacetin is a good substrate of the enzyme . One unit of enzyme activity was determined as the amount of enzyme necessary to produce 1 μM of diacetin per minute under the conditions described above.…”

Section: Methodsmentioning

confidence: 99%

Immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica

Arana-Peña

Lokha

Fernández‐Lafuente

2018

Biotechnology Progress

View full text Add to dashboard Cite

Lipase A from Candida antarctica (CALA, commercialized as Novocor ADL) was immobilized on octyl‐agarose, which is a very useful support for lipase immobilization, and coated with polyethylenimine to improve the stability. The performance was compared to that of the form B of the enzyme (CALB) immobilized on the same support, as both enzymes are among the most popular ones used in biocatalysis. CALA immobilization produced a significant increase in enzyme activity vs. p‐nitrophenyl butyrate (pNPB) (by a factor of seven), and the coating with PEI did not have a significant effect on enzyme activity. CALB reduced its activity slightly after enzyme immobilization. Octyl‐CALA was less stable than octyl‐CALB at pH 9 and more stable at pH 5 and, more clearly, at pH 7. PEI coating only increased octyl‐CALA stability at pH 9. In organic solvents, CALB had much better stability in methanol and was similarly stable in acetonitrile or dioxane. In these systems, the PEI coating of octyl‐CALA permitted some stabilization. While octyl‐CALA was more active vs. pNPB, octyl‐CALB was much more active vs. mandelic esters or triacetin. Thus, depending on the specific reaction and the conditions, CALA or CALB may offer different advantages and drawbacks. © 2018 American Institute of Chemical Engineers Biotechnol. Prog., 35: e2735, 2019

show abstract

Section: Methodsmentioning

confidence: 99%

Immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica

Arana-Peña

Lokha

Fernández‐Lafuente

2018

Biotechnology Progress

View full text Add to dashboard Cite

show abstract

“…65 Concentrations of triacetin were calculated based on calibration curves using real samples. Hydrolysis of triacetin.…”

Section: Preparation Of Core-shell Polymeric Supports and Their Charamentioning

confidence: 99%

Design of a core–shell support to improve lipase features by immobilization

et al. 2016

Self Cite

View full text Add to dashboard Cite

Different core-shell polymeric supports, exhibiting different morphologies and composition, were produced through simultaneous suspension and emulsion polymerization, using styrene (S) and divinylbenzene (DVB) as co-monomers. Supports composed of polystyrene in both the core and the shell (PS/PS) and the new poly(styrene-co-divinylbenzene) support (PS-co-DVB/PS-co-DVB) were used for the immobilization of three different lipases (from Rhizomucor miehie (RML), from Themomyces lanuginosus (TLL) and the form B from Candida antarctica, (CALB)) and of the phospholipase Lecitase Ultra (LU). The features of the new biocatalysts were evaluated and compared to the properties of commercial biocatalysts (Novozym 435 (CALB), Lipozyme RM IM and Lipozyme TL IM) and biocatalysts prepared by enzyme immobilization onto commercial octyl-agarose, a support reported as very suitable for lipase immobilization. It was shown that protein loading and stability of the biocatalysts prepared with the core-shell supports were higher than the ones obtained with commercial octyl-agarose or the commercial lipase preparations. Besides, it was shown that the biocatalysts prepared with the core-shell supports also presented higher activities than commercial biocatalysts when employing different substrates, encouraging the use of the produced core-shell supports for immobilization of lipases and the development of new applications.

show abstract

“…Filamentous fungi are the most widely applied microorganisms in SSF [14]. G. candidum , which is Generally Recognized As Safe (GRAS) [15, 16], has been employed in cheese industry for many years [15].…”

Section: Introductionmentioning

confidence: 99%

Improvement of Medium Chain Fatty Acid Content and Antimicrobial Activity of Coconut Oil via Solid-State Fermentation Using a MalaysianGeotrichum candidum

Khoramnia

Ebrahimpour

Ghanbari

et al. 2013

BioMed Research International

View full text Add to dashboard Cite

Coconut oil is a rich source of beneficial medium chain fatty acids (MCFAs) particularly lauric acid. In this study, the oil was modified into a value-added product using direct modification of substrate through fermentation (DIMOSFER) method. A coconut-based and coconut-oil-added solid-state cultivation using a Malaysian lipolytic Geotrichum candidum was used to convert the coconut oil into MCFAs-rich oil. Chemical characteristics of the modified coconut oils (MCOs) considering total medium chain glyceride esters were compared to those of the normal coconut oil using ELSD-RP-HPLC. Optimum amount of coconut oil hydrolysis was achieved at 29% moisture content and 10.14% oil content after 9 days of incubation, where the quantitative amounts of the modified coconut oil and MCFA were 0.330 mL/g of solid media (76.5% bioconversion) and 0.175 mL/g of solid media (53% of the MCO), respectively. MCOs demonstrated improved antibacterial activity mostly due to the presence of free lauric acid. The highest MCFAs-rich coconut oil revealed as much as 90% and 80% antibacterial activities against Staphylococcus aureus and Escherichia coli, respectively. The results of the study showed that DIMOSFER by a local lipolytic G. candidum can be used to produce MCFAs as natural, effective, and safe antimicrobial agent. The produced MCOs and MCFAs could be further applied in food and pharmaceutical industries.

show abstract

Hydrolysis of triacetin catalyzed by immobilized lipases: Effect of the immobilization protocol and experimental conditions on diacetin yield

Cited by 53 publications

References 32 publications

Immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica

Immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica

Design of a core–shell support to improve lipase features by immobilization

Improvement of Medium Chain Fatty Acid Content and Antimicrobial Activity of Coconut Oil via Solid-State Fermentation Using a MalaysianGeotrichum candidum

Contact Info

Product

Resources

About