Recent progress in multienzymes co-immobilization and multienzyme system applications

Lipases (triacylglycerol hydrolases E.C. 3.1.1.3) are enzymes produced by mammals, plants, fungi and bacteria that catalyze the hydrolysis of triacylglycerols into glycerol and fatty acids. Lipases...

Lipases: From Production to Applications

Dithiocarbamate to modify magnetic graphene oxide nanocomposite (Fe3O4-GO): A new strategy for covalent enzyme (lipase) immobilization to fabrication a new nanobiocatalyst for enzymatic hydrolysis of PNPD.

Different strategies to immobilize lipase from Geotrichum candidum: Kinetic and thermodynamic studies

Eversa is an enzyme recently launched by Novozymes to be used in a free form as biocatalyst in biodiesel production. This paper shows for first time the immobilization of Eversa (a commercial lipase) on octyl and aminated agarose beads and the comparison of the enzyme properties to those of the most used lipase, the isoform B from Candida antarctica (CALB) immobilized on octyl agarose beads. Immobilization on octyl and aminated supports of Eversa has not had a significant effect on enzyme activity versus p-nitrophenyl butyrate (pNPB) under standard conditions (pH 7), but immobilization on octyl agarose beads greatly enhanced the stability of the enzyme under all studied conditions, much more than immobilization on aminated support. Octyl-Eversa was much more stable than octyl-CALB at pH 9, but it was less stable at pH 5. In the presence of 90% acetonitrile or dioxane, octyl-Eversa maintained the activity (even increased the activity) after 45 days of incubation in a similar way to octyl-CALB, but in 90% of methanol, results are much worse, and octyl-CALB became much more stable than Eversa. Coating with PEI has not a clear effect on octyl-Eversa stability, although it affected enzyme specificity and activity response to the changes in the pH. Eversa immobilized octyl supports was more active than CALB versus triacetin or pNPB, but much less active versus methyl mandelate esters. On the other hand, Eversa specificity and response to changes in the medium were greatly modulated by the immobilization protocol or by the coating of the immobilized enzyme with PEI. Thus, Eversa may be a promising biocatalyst for many processes different to the biodiesel production and its properties may be greatly improved following a suitable immobilization protocol, and in some cases is more stable and active than CALB.

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Immobilization of Eversa Lipase on Octyl Agarose Beads and Preliminary Characterization of Stability and Activity Features

Immobilized lipase from Hypocrea pseudokoningii on hydrophobic and ionic supports: Determination of thermal and organic solvent stabilities for applications in the oleochemical industry

The enzymatic transesterification of docosahexaenoic acid (DHA) ethyl ester with glycerol was performed with several lipases in a solvent-free system and it involves the initial formation of sn-2 docosahexaenyl monoacylglyceride. This DHA derivative is highly relevant for improving the bioavailability of DHA and it has received increasing interest in the field of nutrition. Three commercial lipases, from Rhizomucor miehei (RML), Alcaligenes sp (QL), and Candida antarctica-fraction B (CALB) were tested. In certain cases (CALB), using an excess of DHA ethyl ester and high temperatures the transesterification reaction continues to the formation of triacylglycerides, but in other cases, sn-2 monoacylglyceride (2-MG) is the unique synthetic product even in the presence of high concentrations of DHA ethyl ester. At low temperatures (e.g. 37°C), RML derivatives synthesize only 2-MG in 15 min. These very mild conditions are very interesting for the thermal oxidative stability of

https://cogentoa.tandfonline.com/doi/pdf/10.1080/23311932.2016.1164569

FOOD SCIENCE & TECHNOLOGY | SHORT COMMUNICATION Synthesis of sn-2 docosahexaenoyl monoacylglycerol by mild enzymatic transesterification of docosahexaenoic acid ethyl ester and glycerol in a solvent-free system

J. M. Guisan

Papers

Immobilized lipase from Hypocrea pseudokoningii on hydrophobic and ionic supports: Determination of thermal and organic solvent stabilities for applications in the oleochemical industry

FOOD SCIENCE & TECHNOLOGY | SHORT COMMUNICATION Synthesis of sn-2 docosahexaenoyl monoacylglycerol by mild enzymatic transesterification of docosahexaenoic acid ethyl ester and glycerol in a solvent-free system