Synthesis of palmitoleic acid-enriched triacylglycerol via a two-step enzyme reaction
[Display omitted] •Two-step enzyme reaction was performed for synthesis of palmitoleic acid-enriched triacylglycerol.•Palmitoleic acid is enriched efficiently from macadamia nut oil via selective hydrolysis.•Eversa immobilized lipase was prepared by physical binding.•Palmitoleic acid enriched triacy...
Gespeichert in:
Veröffentlicht in: | Process biochemistry (1991) 2022-02, Vol.113, p.234-240 |
---|---|
Hauptverfasser: | , , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
Zusammenfassung: | [Display omitted]
•Two-step enzyme reaction was performed for synthesis of palmitoleic acid-enriched triacylglycerol.•Palmitoleic acid is enriched efficiently from macadamia nut oil via selective hydrolysis.•Eversa immobilized lipase was prepared by physical binding.•Palmitoleic acid enriched triacylglycerol is synthesized successfully using the Eversa immobilized lipase.
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 °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. |
---|---|
ISSN: | 1359-5113 1873-3298 |
DOI: | 10.1016/j.procbio.2022.01.007 |