An uncharacterized protein from the metagenome with no obvious homology to known lipases shows excellent alkaline lipase properties and potential applications in the detergent industry

Xiao, Yumei; Liu, Yi-De; Yuan, Ge; Mao, Runqian; Li, Gang

doi:10.1007/s10529-021-03203-0

Cited by 5 publications

(4 citation statements)

References 34 publications

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“…The recombinant LipGt6 exhibited the highest activity towards medium-and longchain fatty acids (C8-C14). LipGt6 has 12.6% sequence similarity with the lipase Lip486 [17]. Both Lip29 and Lip486 are reported lipases that belong to the GDSL family.…”

Section: Discussionmentioning

confidence: 99%

“…At present, all lipases that can be added to detergents are alkaline, and their optimum pH is 8.0-12.0 [17]. An ideal lipase for detergent addition should have the following characteristics: high activity, high reaction temperature, high pH, and strong resistance to alkali substances, organic solvents, metal ions, and other chemical substances [18].…”

Section: Introductionmentioning

confidence: 99%

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Identification and Characterization of a Novel Thermostable GDSL Lipase LipGt6 from Geobacillus thermoleovorans H9

Qin,

Lin,

Zhan

et al. 2024

Applied Sciences

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Lipases are versatile biocatalysts for various biological reactions. In the detergent industry, lipases must exhibit high activity in environments with high temperature, high pH values, metal ions, and organic solvents. Therefore, researchers are intensively searching for more stable and efficient lipases. A new thermophilic lipase, LipGt6, was identified in Geobacillus thermoleovorans H9, a new thermophilic strain isolated from ultrahigh-temperature compost. A structural model of LipGt6 was constructed using an esterase from Geobacillus thermodenitrificans as a template, and site-directed mutagenesis confirmed the predicted active site residues. LipGt6 exhibited the highest activity towards medium- and long-chain fatty acids (C8–C14), and the optimum temperature and pH were 50 °C and 9.0, respectively. LipGt6 was found to be thermostable up to 70 °C. In the presence of 1% H2O2 and sodium deoxycholate, LipGt6 retained 70 to 75% relative activity. These findings reveal that LipGt6 is potentially useful for the industrial production of detergent. Based on comparison of the amino acid sequences, the enzyme belongs to a new subfamily called lipolytic enzyme family II. The catalytic residues Ser and His were more critical than Asp, and the Asp221 catalytic residue is not likely critical for the lipolytic reaction of LipGt6.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Identification and Characterization of a Novel Thermostable GDSL Lipase LipGt6 from Geobacillus thermoleovorans H9

Qin,

Lin,

Zhan

et al. 2024

Applied Sciences

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“…Wang et al (2018) reported an alkaline, low-temperature, and strong surfactant tolerance recombinant lipase of Trichoderma lentiform ACCC30425 in Pichia pastoris GS115; this lipase is suitable for use in the detergent industry. Xiao et al (2021) also reported a recombinant lipase Lip486 without clear homology alao to know lipase, Lip486 was discovered by using functional metagenomics technology and belongs to a new sub-familycalled lipolytic enzyme family II. The recombinant Lip486 expresses great activity and stability even in alkaline pH and medium-low temperature environments; these properties will make the lipase most important for use in detergent and other industries in the future.…”

Section: In Detergent Manufacturingmentioning

confidence: 99%

Industrial applications of fungal lipases: a review

Kumar¹,

Verma²,

Dubey³

et al. 2023

Front. Microbiol.

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Fungal lipases (triacylglycerol acyl hydrolases EC 3.1.1.3) are significant industrial enzymes and have several applications in a number of industries and fields. Fungal lipases are found in several species of fungi and yeast. These enzymes are carboxylic acid esterases, categorized under the serine hydrolase family, and do not require any cofactor during the catalyzing of the reactions. It was also noticed that processes including the extraction and purification of lipases from fungi are comparatively easier and cheaper than other sources of lipases. In addition, fungal lipases have been classified into three chief classes, namely, GX, GGGX, and Y. Fungal lipases have applications not only in the hydrolysis of fats and oils (triglycerides) but are also involved in synthetic reactions such as esterification, acidolysis, alcoholysis, interesterification, and aminolysis. The production and activity of fungal lipases are highly affected by the carbon source, nitrogen source, temperature, pH, metal ions, surfactants, and moisture content. Therefore, fungal lipases have several industrial and biotechnological applications in many fields such as biodiesel production, ester synthesis, production of biodegradable biopolymers, formulations of cosmetics and personal care products, detergent manufacturing, degreasing of leather, pulp and paper production, textile industry, biosensor development, and drug formulations and as a diagnostic tool in the medical sector, biodegradation of esters, and bioremediation of wastewater. The immobilization of fungal lipases onto different carriers also helps in improving the catalytic activities and efficiencies of lipases by increasing thermal and ionic stability (in organic solvents, high pH, and temperature), being easy to recycle, and inducing the volume-specific loading of the enzyme onto the support, and thus, these features have proved to be appropriate for use as biocatalysts in different sectors.

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“…Unfortunately, in numerous instances, the characteristics of lipases (like other enzymes) do not meet the requirements of industrial catalysts, and their catalytic performance in industrial reactions is inadequate. Currently, there are numerous strategies to address some of the problems with lipases, using metagenomics (searching for beneficial enzymes) (Xiao et al 2021 ), site-directed mutagenesis (Maldonado et al 2023 ; Min et al 2021 ; Wang et al 2021a ), directed evolution (Li et al 2021 ), and chemical modification (Cavalcante et al 2022 ). Protein engineering strategies that utilize genetic mutation based on resolved lipase crystal structures can effectively modify lipase activity and stability (Lan et al 2021 ).…”

Section: Introductionmentioning

confidence: 99%

Characterization of a recombinant Aspergillus niger GZUF36 lipase immobilized by ionic liquid modification strategy

Xing,

Long,

Xie

et al. 2024

Appl Microbiol Biotechnol

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Enzyme immobilized on magnetic nanomaterials is a promising biocatalyst with efficient recovery under applied magnets. In this study, a recombinant extracellular lipase from Aspergillus niger GZUF36 (PEXANL1) expressed in Pichia pastoris GS115 was immobilized on ionic liquid-modified magnetic nano ferric oxide (Fe3O4@SiO2@ILs) via electrostatic and hydrophobic interaction. The morphology, structure, and properties of Fe3O4@SiO2@ILs and immobilized PEXANL1 were characterized by scanning electron microscopy, Fourier transform infrared spectroscopy, x-ray diffraction, vibration sample magnetometer, and zeta potential analysis. Under optimized conditions, the immobilization efficiency and activity recovery of immobilized PEXANL1 were 52 ± 2% and 122 ± 2%, respectively. The enzymatic properties of immobilized PEXANL1 were also investigated. The results showed that immobilized PEXANL1 achieved the maximum activity at pH 5.0 and 45 °C, and the lipolytic activity of immobilized PEXANL1 was more than twice that of PEXANL1. Compared to PEXANL1, immobilized PEXANL1 exhibited enhanced tolerance to temperature, metal ions, surfactants, and organic solvents. The operation stability experiments revealed that immobilized PEXANL1 maintained 86 ± 3% of its activity after 6 reaction cycles. The enhanced catalytic performance in enzyme immobilization on Fe3O4@SiO2@ILs made nanobiocatalysts a compelling choice for bio-industrial applications. Furthermore, Fe3O4@SiO2@ILs could also benefit various industrial enzymes and their practical uses. Key points • Immobilized PEXANL1 was confirmed by SEM, FT-IR, and XRD. • The specific activity of immobilized PEXANL1 was more than twice that of PEXANL1. • Immobilized PEXANL1 had improved properties with good operational stability. Graphical abstract

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An uncharacterized protein from the metagenome with no obvious homology to known lipases shows excellent alkaline lipase properties and potential applications in the detergent industry

Cited by 5 publications

References 34 publications

Identification and Characterization of a Novel Thermostable GDSL Lipase LipGt6 from Geobacillus thermoleovorans H9

Identification and Characterization of a Novel Thermostable GDSL Lipase LipGt6 from Geobacillus thermoleovorans H9

Industrial applications of fungal lipases: a review

Characterization of a recombinant Aspergillus niger GZUF36 lipase immobilized by ionic liquid modification strategy

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