Characterization of a novel thermostable phospholipase C from T. kodakarensis suitable for oil degumming
The implementation of cleaner technologies that minimize environmental pollution caused by conventional industrial processes is an increasing global trend. Hence, traditionally used chemicals have been replaced by novel enzymatic alternatives in a wide variety of industrial-scale processes. Enzymati...
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Veröffentlicht in: | Applied microbiology and biotechnology 2022-08, Vol.106 (13-16), p.5081-5091 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | The implementation of cleaner technologies that minimize environmental pollution caused by conventional industrial processes is an increasing global trend. Hence, traditionally used chemicals have been replaced by novel enzymatic alternatives in a wide variety of industrial-scale processes. Enzymatic oil degumming, the first step of the oil refining process, exploits the conversion catalyzed by phospholipases to remove vegetable crude oils’ phospholipids. This enzymatic method reduces the gums’ volume and increases the overall oil yield. A thermostable phospholipase would be highly advantageous for industrial oil degumming as oil treatment at higher temperatures would save energy and increase the recovery of oil by facilitating the mixing and gums removal. A thermostable phosphatidylcholine (PC) (and phosphatidylethanolamine (PE))-specific phospholipase C from
Thermococcus kodakarensis
(
Tk
PLC) was studied and completely removed PC and PE from crude soybean oil at 80 °C. Due to these characteristics,
Tk
PLC is an interesting promising candidate for industrial-scale enzymatic oil degumming at high temperatures.
Key points
• A thermostable phospholipase C from T. kodakarensis (TkPLC) has been identified.
• TkPLC was recombinantly produced in Pichia pastoris and successfully purified.
• TkPLC completely hydrolyzed PC and PE in soybean oil degumming assays at 80 °C. |
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ISSN: | 0175-7598 1432-0614 |
DOI: | 10.1007/s00253-022-12081-z |