2000Journal of Food LipidsRequires access

LIPASE‐CATALYZED PRODUCTION OF STRUCTURED LIPIDS VIA ACIDOLYSIS OF FISH OIL WITH CAPRYLIC ACID

Dequan Zhou, Xuebing Xu, Huiling Mu, Carl‐Erik Høy, Jens Adler‐Nissen

Open publisher page 18 citations

Abstract

ABSTRACT Structured lipids containing eicosapentaenoic and docosahexaenoic acids were manufactured in a batch reactor by lipase‐catalyzed acidolysis of fish oil with caprylic acid. The following free lipases (Lipase AP, Aspergillus niger; Lipase P, Pseudomonus sp.; Lipase AY, Candida rugosa; Lipase AK, Pseudomonas fluoresescens; Lipase F, Rhizopus oryzae; Lipase D, Rhizopus delemar) were screened under selected reaction conditions. The conditions were enzyme load 5%, substrate mole ratio 1:6 (fish oil: caprylic acid), and reaction temperature of 50C. Lipase AK had the highest activity and was suitable for production of structured lipids from fish oil. The optimal mole substrate ratio of fish oil to caprylic acid for Lipase AK was 1:6 to 1:8. The time course of the reaction at different enzyme loads demonstrated that 40% incorporation of caprylic acid could be obtained for Lipase AK in 5 h with 10% enzyme load. Addition of water had little effect on the activity of the lipase. Lipase AK and Lipozyme IM were further compared under the same conditions, in which Lipase AK had a slightly higher incorporation of caprylic acid, similar acyl migration of caprylic acid from sn‐1,3 positions to the sn‐2 position, and a slightly lower selectivity towards docosahexaenoic acid.

About this research paper

What this paper is about

ABSTRACT Structured lipids containing eicosapentaenoic and docosahexaenoic acids were manufactured in a batch reactor by lipase‐catalyzed acidolysis of fish oil with caprylic acid. The following free lipases (Lipase AP, Aspergillus niger; Lipase P, Pseudomonus sp.; Lipase AY, Candida rugosa; Lipase AK, Pseudomonas fluoresescens; Lipase F, Rhizopus oryzae; Lipase D, Rhizopus delemar) were screened under selected reaction conditions. The conditions were enzyme load 5%, substrate mole ratio 1:6 (fish oil: caprylic acid), and reaction temperature of 50C. Lipase AK had the highest activity and was suitable for production of structured lipids from fish oil. The optimal mole substrate ratio of fish oil to caprylic acid for Lipase AK was 1:6 to 1:8. The time course of the reaction at different enzyme loads demonstrated that 40% incorporation of caprylic acid could be obtained for Lipase AK in 5 h with 10% enzyme load. Addition of water had little effect on the activity of the lipase. Lipase AK and Lipozyme IM were further compared under the same conditions, in which Lipase AK had a slightly higher incorporation of caprylic acid, similar acyl migration of caprylic acid from sn‐1,3 positions to the sn‐2 position, and a slightly lower selectivity towards docosahexaenoic acid.

Why it matters

OpenAlex reports 18 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

ABSTRACT Structured lipids containing eicosapentaenoic and docosahexaenoic acids were manufactured in a batch reactor by lipase‐catalyzed acidolysis of fish oil with caprylic acid. The following free lipases (Lipase AP, Aspergillus niger; Lipase P, Pseudomonus sp.; Lipase AY, Candida rugosa; Lipase AK, Pseudomonas fluoresescens; Lipase F, Rhizopus oryzae; Lipase D, Rhizopus delemar) were screened under selected reaction conditions. The conditions were enzyme load 5%, substrate mole ratio 1:6 (fish oil: caprylic acid), and reaction temperature of 50C. Lipase AK had the highest activity and was suitable for production of structured lipids from fish oil. The optimal mole substrate ratio of fish oil to caprylic acid for Lipase AK was 1:6 to 1:8. The time course of the reaction at different enzyme loads demonstrated that 40% incorporation of caprylic acid could be obtained for Lipase AK in 5 h with 10% enzyme load. Addition of water had little effect on the activity of the lipase. Lipase AK and Lipozyme IM were further compared under the same conditions, in which Lipase AK had a slightly higher incorporation of caprylic acid, similar acyl migration of caprylic acid from sn‐1,3 positions to the sn‐2 position, and a slightly lower selectivity towards docosahexaenoic acid.

Key concepts: Caprylic acid, Lipase, Chemistry, Substrate (aquarium), Docosahexaenoic acid, Fish oil, Interesterified fat, Eicosapentaenoic acid

Related papers

Back to paper searchBrowse research topicsOriginal source
LIPASE‐CATALYZED PRODUCTION OF STRUCTURED LIPIDS VIA ACIDOLYSIS OF FISH OIL WITH CAPRYLIC ACID — Research Paper | ScholarLens