Academic Journal

A novel cold-adapted esterase from Lysinibacillus pakistanensis VF-2 for efficient degradation of pyrethroid residues in tea leaves.

Λεπτομέρειες βιβλιογραφικής εγγραφής
Τίτλος: A novel cold-adapted esterase from Lysinibacillus pakistanensis VF-2 for efficient degradation of pyrethroid residues in tea leaves.
Συγγραφείς: Wang W; School of Food and Bioengineering, Xihua University, Chengdu 610039, Sichuan, China., Zhou H; School of Food and Bioengineering, Xihua University, Chengdu 610039, Sichuan, China., Tang J; School of Food and Bioengineering, Xihua University, Chengdu 610039, Sichuan, China; Food Microbiology Key Laboratory of Sichuan Province, Xihua University, Chengdu 610039, Sichuan, China; Chongqing Key Laboratory of Speciality Food Co-Built by Sichuan and Chongqing, Xihua University, Chengdu 610039, China. Electronic address: tangjie1225@xhu.edu.cn., Huang S; School of Food and Bioengineering, Xihua University, Chengdu 610039, Sichuan, China., Zhang M; School of Food and Bioengineering, Xihua University, Chengdu 610039, Sichuan, China; Food Microbiology Key Laboratory of Sichuan Province, Xihua University, Chengdu 610039, Sichuan, China., Zhang Y; School of Food and Bioengineering, Xihua University, Chengdu 610039, Sichuan, China., Lei L; School of Food and Bioengineering, Xihua University, Chengdu 610039, Sichuan, China., Chen S; School of Food and Bioengineering, Xihua University, Chengdu 610039, Sichuan, China., Wen Q; School of Food and Bioengineering, Xihua University, Chengdu 610039, Sichuan, China., Liu Y; School of Food and Bioengineering, Xihua University, Chengdu 610039, Sichuan, China., Xiang W; School of Food and Bioengineering, Xihua University, Chengdu 610039, Sichuan, China; Food Microbiology Key Laboratory of Sichuan Province, Xihua University, Chengdu 610039, Sichuan, China., Zhang Q; School of Food and Bioengineering, Xihua University, Chengdu 610039, Sichuan, China; Food Microbiology Key Laboratory of Sichuan Province, Xihua University, Chengdu 610039, Sichuan, China., Yu X; School of Food and Bioengineering, Xihua University, Chengdu 610039, Sichuan, China; Food Microbiology Key Laboratory of Sichuan Province, Xihua University, Chengdu 610039, Sichuan, China. Electronic address: yuxuan152@xhu.edu.cn.
Πηγή: Pesticide biochemistry and physiology [Pestic Biochem Physiol] 2026 Sep; Vol. 223, pp. 107292. Date of Electronic Publication: 2026 Aug 13.
Τύπος έκδοσης: Journal Article
Γλώσσα: English
Στοιχεία περιοδικού: Publisher: Academic Press Country of Publication: United States NLM ID: 1301573 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1095-9939 (Electronic) Linking ISSN: 00483575 NLM ISO Abbreviation: Pestic Biochem Physiol Subsets: MEDLINE
Imprint Name(s): Original Publication: New York Ny : Academic Press
Ιατρικοί όροι (MeSH): Pyrethrins*/metabolism , Esterases*/metabolism , Esterases*/genetics , Bacillaceae*/enzymology , Bacillaceae*/genetics , Pesticide Residues*/metabolism , Tea*/chemistry, Plant Leaves/chemistry ; Plant Leaves/metabolism ; Bacterial Proteins/metabolism ; Bacterial Proteins/genetics ; Insecticides/metabolism ; Cold Temperature ; Biodegradation, Environmental ; Amino Acid Sequence
Περίληψη: Pyrethroid residues in tea have emerged as a significant safety concern due to their high lipophilicity and persistence, while efficient and mild enzymatic removal resources remain scarce. In this study, two novel esterase genes, gene3341 and gene2566, were identified from Lysinibacillus pakistanensis VF-2, both belonging to the α/β-hydrolase superfamily with a typical catalytic triad and conserved Gly-X-Ser-X-Gly motif. The recombinant enzymes Est3341 and Est2566 were successfully expressed in Escherichia coli, and exhibited β-cypermethrin (β-CY) degradation efficiencies of 77.97% and 71.92% within 7 days, respectively. Biochemical characterization demonstrated that Est3341 was a cold-adapted esterase with optimal activity at 25 °C and pH 7.0, enabling efficient degradation under mild conditions suitable for heat-sensitive tea matrices. Notably, Est3341 degraded 98.68% of high-concentration β-CY within 36 h, and its activity was significantly enhanced by Ca2+ and Mn2+. In tea leaf application, Est3341 removed 55.01% of β-CY, 59.40% of cypermethrin, and 46.23% of deltamethrin residues within 20 min at 25 °C. GC-MS analysis revealed that Est3341 hydrolyzed β-CY's ester bonds to yield 3-phenoxybenzaldehyde and other characteristic intermediates. This study provides a high-efficiency, mild-condition, tea-adapted esterase resource for green removal of pyrethroid residues in agricultural products, offering a promising strategy for food safety and environmental bioremediation.
(Copyright © 2026. Published by Elsevier Inc.)
Competing Interests: Declaration of competing interest All authors declare that there are not any financial and personal relationships with other people or organizations that could inappropriately influence this work. There are not any potential conflicts of interest include employment, consultancies, stock ownership, honoraria, paid expert testimony, patent applications/ registrations, and grants or other funding. All the authors mutually agree to submit to your journal. The authors declare that they have no competing financial interests.
Contributed Indexing: Keywords: Biodegradation; Esterase; Lysinibacillus; Pesticide residues; Pyrethroid degradation
Substance Nomenclature: 0 (Pyrethrins)
EC 3.1.- (Esterases)
0 (Pesticide Residues)
1TR49121NP (cypermethrin)
0 (Tea)
0 (Bacterial Proteins)
0 (Insecticides)
Entry Date(s): Date Created: 20260904 Date Completed: 20260904 Latest Revision: 20260904
Update Code: 20260905
DOI: 10.1016/j.pestbp.2026.107292
PMID: 42697661
Βάση Δεδομένων: MEDLINE
Περιγραφή
ISSN:1095-9939
DOI:10.1016/j.pestbp.2026.107292