Substrate specificities of lipases in view of kinetic resolution of unsaturated fatty acids

Mukherjee, Kumar D.; Kiewitt, Irmgard; Hills, Matthew J.

doi:10.1007/bf00175736

Cited by 57 publications

(43 citation statements)

References 17 publications

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“…There have been many attempts to employ lipase-catalyzed hydrolysis to produce omega 3 PUFA concentrates. Several studies showed that the efficiency of concentration depended on the substrate specificity, both acyl chain and molecule specificities, of the lipase used [4][5][6][7][8][9][10][11][12].…”

Section: Introductionmentioning

confidence: 99%

Upgrading of Farmed Salmon Oil Through Lipase-Catalyzed Hydrolysis

Kahveci¹,

Falkeborg²,

Gregersen³

et al. 2010

TOBIOTJ

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Upgrading of farmed salmon oil obtained from by-products was carried out by lipase-catalyzed hydrolysis to increase omega 3 polyunsaturated fatty acids (PUFA) content. The lipases tested were from Penicillium camembertii (PC), Rhizomucor javanicus (RJ), Rhizopus niveus (RN), Rhizopus delemar (RD), Burkholderia cepacia (BC), Rhizopus oryzae (RO), Candida rugosa (CR) and Rhizomucor miehei (RM). The lipases from PC, RJ and RN had lower hydrolysis degrees (HDs) compared to the rest of the lipases. The lipase from CR had the highest HD after 24 h (91.89%). Moreover, CR lipase was the most effective one in concentrating omega 3 PUFA. The final value was increased from 13.77% to 27.81% (wt%). The changes in omega 3 PUFA content were significantly different among the lipases although the HD values were similar at the end of the reactions, which was believed to be caused by the substrate specificities of the lipases. The investigation of the relationship between HD and hydrolysis resistant value (HRV) for eicosapentaenoic acid (EPA, 20:5), docosahexaenoic acid (DHA, 22:6) and oleic acid (OA, 18:1) revealed that the fatty acid (FA) selectivity of the lipases were significantly different. CR lipase had the highest preference for hydrolyzing OA selectively over EPA and DHA. The reaction conditions, i.e. presence of surfactants, sonication, buffer-to-oil ratio, enzyme load, did not affect the selectivity. Investigation of the reaction conditions revealed that it was possible to obtain ~2.15-fold of the original omega 3 PUFA content by hydrolysis of salmon oil in the presence of CR lipase (4%, based on oil weight) with a bufferto-oil ratio of 2:1 (v/v) at 37 o C for 4 h.

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Section: Introductionmentioning

confidence: 99%

Upgrading of Farmed Salmon Oil Through Lipase-Catalyzed Hydrolysis

Kahveci¹,

Falkeborg²,

Gregersen³

et al. 2010

TOBIOTJ

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“…However, many of the lipases discriminate against polyunsaturated fatty acids [9][10][11], and DHA is usually the fatty acid that is discriminated most. EPA has successfully been incorporated into phospholipids using Rhizomucor miehei lipase (Lipozyme) as catalyst at temperatures of 40-65 7C [12,13], while on the other hand, incorporation of DHA at the sn-1 position of phosphatidylcholine (PC) has been found to be low [14] unless the temperature is elevated to 60 7C [13], with the drawback of considerable acyl migration.…”

Section: Introductionmentioning

confidence: 99%

Enzymatic and chemical synthesis of phosphatidylcholine regioisomers containing eicosapentaenoic acid or docosahexaenoic acid

Lyberg

Adlercreutz

2005

Euro J Lipid Sci & Tech

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Regioselective incorporation of eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) into phosphatidylcholine (PC) was carried out using enzymatic and chemical synthesis. Incorporation at the sn-1 position was successfully achieved by lipasecatalysed esterification of 2-palmitoyl-lysophosphatidylcholine (LPC), although in most cases, the enzymes incorporated EPA and DHA at lower rates than other fatty acids. For the incorporation of DHA, Candida antarctica lipase B was the only useful enzyme, while incorporation of EPA was efficiently carried out using either this enzyme or Rhizopus arrhizus lipase. The highest yields in the lipase-catalysed reactions were obtained at the lowest water activity (close to 0). However, by carrying out the reactions at a higher water activity of 0.22, more EPA and DHA were incorporated. Esterification of 2-palmitoyl-LPC with pure EPA at this water activity converted 66 mol-% of LPC to PC using Rhizopus arrhizus lipase as catalyst. When the fatty acid was DHA and the catalyst Candida antarctica lipase B, 45 mol-% of PC was obtained. For incorporation of EPA and DHA at the sn-2 position, phospholipase A 2 was used, but the reaction was very slow. Chemical coupling of 1-palmitoyl-LPC and EPA or DHA was more efficient, resulting in complete conversion of LPC.

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“…Because the transacylation ratio indicates the efficacy of We demonstrated substrate specificity of lipase OF on PUFAs. Mukherjiee et al examined the esterification of several fatty acids with 1-butanol and showed that lipases from Penicillium cyclopium and C. cylindracea recognized fatty acids to varying degrees, with the first double bond from the carboxyl end as a C5 EPA, C20:5 n-3 C6 C18:1 n-12, C18:3 n-6, C18:4 n-6 C4 DHA, C 22:6 n-3 17 . HPA and DPA have the first double bond from carboxyl end at C6 and C7, respectively.…”

Section: Resultsmentioning

confidence: 99%