Auto-induction, biochemical characterization and application of a novel thermo-alkaline and detergent-stable lipase (S9 peptidase domain) from Thermotoga petrophila as cleaning additive and degrading oil/fat wastes

Akram, Fatima; Fatima, Taseer; ul Haq, Ikram

doi:10.1016/j.bioorg.2024.107658

Bioorganic Chemistry

2024

DOI: 10.1016/j.bioorg.2024.107658

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Auto-induction, biochemical characterization and application of a novel thermo-alkaline and detergent-stable lipase (S9 peptidase domain) from Thermotoga petrophila as cleaning additive and degrading oil/fat wastes

Fatima Akram,

Taseer Fatima,

Ikram ul Haq

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Cited by 2 publications

References 45 publications

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Enzymatic modification of cotton fibre polysaccharides as an enabler of sustainable laundry detergents

Yau,

Byard,

Thompson

et al. 2024

Sci Rep

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Cotton is the most common natural fibre used in textile manufacture, used alone or with other fibres to create a wide range of fashion clothing and household textiles. Most of these textiles are cleaned using detergents and domestic or commercial washing machines using processes that require many chemicals and large quantities of water and energy. Enzymes can reduce this environmental footprint by enabling effective detergency at reduced temperatures, mostly by directly attacking substrates present in the soils. In the present study, we report the contribution of a cleaning cellulase enzyme based on the family 44 glycoside hydrolase (GH) endo-beta-1,4-glucanase from Paenibacillus polymyxa. The action of this enzyme on textile fibres improves laundry detergent performance in several vectors including soil anti-redeposition, dye transfer inhibition and stain removal. Molecular probes are used to study how this enzyme is targeting both amorphous cellulose and xyloglucan on textile fibres and the relationship between textile surface effects and observed performance benefits.

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Enzymatic modification of cotton fibre polysaccharides as an enabler of sustainable laundry detergents

Yau,

Byard,

Thompson

et al. 2024

Sci Rep

View full text Add to dashboard Cite

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A Lipase Gene of Thermomyces lanuginosus: Sequence Analysis and High-Efficiency Expression in Pichia pastoris

Yi,

Cheng,

Yang

et al. 2024

IJMS

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Lipase, a type of enzyme that decomposes and synthesizes triglycerides, plays an important role in lipid processing. In this study, a heat-resisting lipase gene (lip4) from Thermomyces lanuginosus was subcloned into the pPICZαA vector and then transformed into Pichia pastoris X33. The recombinant yeast cell concentration reached the maximum (119.5 g/L) at 144 h, and the lipase (Lip4) activity reached the maximum (3900 U/mL) at 168 h in 10 L bioreactor. Through bioinformatics analysis, S168, as the key site of Lip4, participated in the formation of the catalytic triads S168-D223-H280 and G166-H167-S168-L169-G170. Furthermore, S168 and seven conserved amino acids of G104/288, S105, A195, P196, V225 and I287 constitute the active center of Lip4. Specifically, the structure modeling showed two α-helices of the lid domain, outside the active pocket domain, controlling the entry of the substrate on Lip4. The potential glycosylation of Asn-33 may be involved in exhibiting the high stable temperature for lipase activity. Therefore, the eukaryotic system was constructed to express Lip4 efficiently, and the amino acid sites related to the catalytic efficiency of Lip4 were clarified, providing a new way for its subsequent property research and industrial application.

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Auto-induction, biochemical characterization and application of a novel thermo-alkaline and detergent-stable lipase (S9 peptidase domain) from Thermotoga petrophila as cleaning additive and degrading oil/fat wastes

Cited by 2 publications

References 45 publications

Enzymatic modification of cotton fibre polysaccharides as an enabler of sustainable laundry detergents

Enzymatic modification of cotton fibre polysaccharides as an enabler of sustainable laundry detergents

A Lipase Gene of Thermomyces lanuginosus: Sequence Analysis and High-Efficiency Expression in Pichia pastoris

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