Synthesis of palmitoleic acid-enriched triacylglycerol via a two-step enzyme reaction
- 주제(키워드) Candida rugosa lipase , Esterification , Eversa lipase , Macadamia nut oil , Palmitoleic acid (POA) , Selective hydrolysis , Triacylglycerol (TAG)
- 주제(기타) Biochemistry & Molecular Biology
- 주제(기타) Biotechnology & Applied Microbiology
- 주제(기타) Engineering, Chemical
- 설명문(일반) [Oh, Dongchan; Kim, Yangha; Kim, In-Hwan] Korea Univ, Grad Sch, Dept Integrated Biomed & Life Sci, Seoul 02841, South Korea; [No, Da Som] Rutgers State Univ, Sch Environm & Biol Sci, New Brunswick, NJ 08902 USA; [Kim, Yangha] Ewha Womans Univ, Dept Nutr Sci & Food Management, Seoul 03760, South Korea; [Kim, Hak-Ryul] Kyungpook Natl Univ, Sch Food Sci & Biotechnol, Daegu 41566, South Korea; [Kim, In-Hwan] Korea Univ, Grad Sch, Dept Integrated Biomed & Life Sci, 145 Anam-Ro, Seoul, South Korea; [Kim, In-Hwan] Korea Univ, BK21FOUR R&E Ctr Learning Hlth Syst, Seoul, South Korea
- 등재 SCIE, SCOPUS
- 발행기관 ELSEVIER SCI LTD
- 발행년도 2022
- URI http://www.dcollection.net/handler/ewha/000000190403
- 본문언어 영어
- Published As https://doi.org/10.1016/j.procbio.2022.01.007
초록/요약
Palmitoleic acid (POA) is known to have various biological activities in animal models. POA-enriched triacylglycerol (TAG) was successfully synthesized using a two-step enzyme reaction. First, the POA-enriched fatty acid obtained from macadamia nut oil by Candida rugosa lipase-catalyzed selective hydrolysis was employed as a substrate for the synthesis of POA-enriched TAG. Two parameters such as temperature and enzyme loading, were optimized to enrich POA by the selective hydrolysis. For the TAG synthesis, liquid Eversa lipase was immobilized in house on Lewatit VP OC 1600 as a carrier and the protein content in the carrier was 130 mg/ g carrier. The degree of synthesis of POA-enriched TAG using Eversa immobilized lipase prepared in house was investigated in comparison to three commercial lipases and Eversa immobilized lipase demonstrated a superior activity in TAG conversion. The effects of temperature, enzyme loading, and vacuum on the synthesis of POA-enriched TAG using the Eversa immobilized lipase were investigated. The optimum conditions were a temperature of 60 degrees C, an enzyme loading of 12.5 %, and a vacuum of 100 torr. The maximum TAG conversion was ca. 89 % after 12 h under the optimum conditions.
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