A New Enzyme for Biodiesel Production and Food Applications: Lipase of Bacillus megaterium F25 Isolated From an Aquatic Insect Rhantus suturalis

ABSTRACT This study aimed to isolate, purify, and characterize a lipase from the gut symbiont Bacillus megaterium F25 (GenBank accession: MF597792) of the aquatic insect Rhantus suturalis, with a focus on its potential applications in biodiesel and food industries. Under optimized culture conditions...

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Main Authors: Fatima Karaman, Umit Incekara, Nazli Pinar Arslan, Seyda Albayrak, Serkan Ortucu, Mesut Taskin
Format: Article
Language:English
Published: Wiley 2024-12-01
Series:GCB Bioenergy
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Online Access:https://doi.org/10.1111/gcbb.70009
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author Fatima Karaman
Umit Incekara
Nazli Pinar Arslan
Seyda Albayrak
Serkan Ortucu
Mesut Taskin
author_facet Fatima Karaman
Umit Incekara
Nazli Pinar Arslan
Seyda Albayrak
Serkan Ortucu
Mesut Taskin
author_sort Fatima Karaman
collection DOAJ
description ABSTRACT This study aimed to isolate, purify, and characterize a lipase from the gut symbiont Bacillus megaterium F25 (GenBank accession: MF597792) of the aquatic insect Rhantus suturalis, with a focus on its potential applications in biodiesel and food industries. Under optimized culture conditions, B. megaterium F25 could produce 583 U/L of lipase in shaking flask culture. The purified lipase (PL) exhibited a specific activity with 113.89 U/mg, and its molecular weight was determined as 34 kDa. The activity of PL was enhanced by methanol, ethanol, Tween‐80, Triton X‐100, Ca2+, and Mg2+, while β‐mercaptoethanol, EDTA, SDS, Fe2+, Mn2+, and Cu2+ were inhibitory. PL showed optimal activity and stability at neutral and slightly acidic pHs, as well as in a temperature range of 20°C–30°C. PL displayed strong hydrolytic activity toward plant oils and animal fats, indicating its potency for both the food industry and the remediation of oil‐contaminated environments. When tested as a catalyst, PL provided biodiesel production with a transesterification yield of 86.8% under optimized conditions (36 h reaction time, 4 mL enzyme solution, 30°C, pH 7.0, and waste cooking oil:methanol ratio of 10 mL/40 mL). This is the first report on the lipase‐producing potential of gut microbial symbionts of aquatic insects. Furthermore, B. megaterium lipase was tested for the first time as a biocatalyst for biodiesel production.
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spelling doaj-art-a96b8fd3d4964f60b74d66240c2e95492024-11-27T09:32:31ZengWileyGCB Bioenergy1757-16931757-17072024-12-011612n/an/a10.1111/gcbb.70009A New Enzyme for Biodiesel Production and Food Applications: Lipase of Bacillus megaterium F25 Isolated From an Aquatic Insect Rhantus suturalisFatima Karaman0Umit Incekara1Nazli Pinar Arslan2Seyda Albayrak3Serkan Ortucu4Mesut Taskin5Department of Biology, Science Faculty Ataturk University Erzurum TurkeyDepartment of Biology, Science Faculty Ataturk University Erzurum TurkeyVocational School of Health Services Bingol University Bingol TurkeyDepartment of Molecular Biology and Genetics, Science Faculty Ataturk University Erzurum TurkeyDepartment of Molecular Biology and Genetics, Science Faculty Erzurum Technical University Erzurum TurkeyDepartment of Molecular Biology and Genetics, Science Faculty Ataturk University Erzurum TurkeyABSTRACT This study aimed to isolate, purify, and characterize a lipase from the gut symbiont Bacillus megaterium F25 (GenBank accession: MF597792) of the aquatic insect Rhantus suturalis, with a focus on its potential applications in biodiesel and food industries. Under optimized culture conditions, B. megaterium F25 could produce 583 U/L of lipase in shaking flask culture. The purified lipase (PL) exhibited a specific activity with 113.89 U/mg, and its molecular weight was determined as 34 kDa. The activity of PL was enhanced by methanol, ethanol, Tween‐80, Triton X‐100, Ca2+, and Mg2+, while β‐mercaptoethanol, EDTA, SDS, Fe2+, Mn2+, and Cu2+ were inhibitory. PL showed optimal activity and stability at neutral and slightly acidic pHs, as well as in a temperature range of 20°C–30°C. PL displayed strong hydrolytic activity toward plant oils and animal fats, indicating its potency for both the food industry and the remediation of oil‐contaminated environments. When tested as a catalyst, PL provided biodiesel production with a transesterification yield of 86.8% under optimized conditions (36 h reaction time, 4 mL enzyme solution, 30°C, pH 7.0, and waste cooking oil:methanol ratio of 10 mL/40 mL). This is the first report on the lipase‐producing potential of gut microbial symbionts of aquatic insects. Furthermore, B. megaterium lipase was tested for the first time as a biocatalyst for biodiesel production.https://doi.org/10.1111/gcbb.70009aquatic insectsgut symbiontlipaselipolytic bacteriatransesterification
spellingShingle Fatima Karaman
Umit Incekara
Nazli Pinar Arslan
Seyda Albayrak
Serkan Ortucu
Mesut Taskin
A New Enzyme for Biodiesel Production and Food Applications: Lipase of Bacillus megaterium F25 Isolated From an Aquatic Insect Rhantus suturalis
GCB Bioenergy
aquatic insects
gut symbiont
lipase
lipolytic bacteria
transesterification
title A New Enzyme for Biodiesel Production and Food Applications: Lipase of Bacillus megaterium F25 Isolated From an Aquatic Insect Rhantus suturalis
title_full A New Enzyme for Biodiesel Production and Food Applications: Lipase of Bacillus megaterium F25 Isolated From an Aquatic Insect Rhantus suturalis
title_fullStr A New Enzyme for Biodiesel Production and Food Applications: Lipase of Bacillus megaterium F25 Isolated From an Aquatic Insect Rhantus suturalis
title_full_unstemmed A New Enzyme for Biodiesel Production and Food Applications: Lipase of Bacillus megaterium F25 Isolated From an Aquatic Insect Rhantus suturalis
title_short A New Enzyme for Biodiesel Production and Food Applications: Lipase of Bacillus megaterium F25 Isolated From an Aquatic Insect Rhantus suturalis
title_sort new enzyme for biodiesel production and food applications lipase of bacillus megaterium f25 isolated from an aquatic insect rhantus suturalis
topic aquatic insects
gut symbiont
lipase
lipolytic bacteria
transesterification
url https://doi.org/10.1111/gcbb.70009
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