Has the time finally come for green oleochemicals and biodiesel production using large-scale enzyme technologies? Current status and new developments

Biotechnology Advances, Journal Year: 2023, Volume and Issue: 69, P. 108275 - 108275

Published: Oct. 30, 2023

Language: Английский

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Recent applications and future prospects of magnetic biocatalysts

International Journal of Biological Macromolecules, Journal Year: 2023, Volume and Issue: 253, P. 126709 - 126709

Published: Sept. 9, 2023

Language: Английский

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Demystifying the enzymatic biodiesel: How lipases are contributing to its technological advances

Renewable Energy, Journal Year: 2023, Volume and Issue: 216, P. 119085 - 119085

Published: July 26, 2023

Language: Английский

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Impact of aroma-enhancing microorganisms on aroma attributes of industrial Douchi: An integrated analysis using E-nose, GC-IMS, GC–MS, and descriptive sensory evaluation

Food Research International, Journal Year: 2024, Volume and Issue: 182, P. 114181 - 114181

Published: March 4, 2024

Language: Английский

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A comprehensive review of lipase-catalyzed acidolysis as a method for producing structured glycerides

International Journal of Biological Macromolecules, Journal Year: 2025, Volume and Issue: unknown, P. 142878 - 142878

Published: April 1, 2025

Language: Английский

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A novel endo-1,4-β-xylanase from Alicyclobacillus mali FL18: Biochemical characterization and its synergistic action with β-xylosidase in hemicellulose deconstruction

International Journal of Biological Macromolecules, Journal Year: 2024, Volume and Issue: 264, P. 130550 - 130550

Published: March 1, 2024

A novel endo-1,4-β-xylanase-encoding gene was identified in Alicyclobacillus mali FL18 and the recombinant protein, named AmXyn, purified biochemically characterized. The monomeric enzyme worked optimally at pH 6.6 80 °C on beechwood xylan with a specific activity of 440.00 ± 0.02 U/mg good catalytic efficiency (kcat/KM = 91.89 s−1mLmg−1). In addition, did not display any cellulose, suggesting possible application paper biobleaching processes. To develop an enzymatic mixture for degradation, association between AmXyn previously characterized β-xylosidase AmβXyl, deriving from same microorganism, assessed. two enzymes had similar temperature optima showed highest degree synergy when AmβXyl were added sequentially to xylan, making this cost-competitive suitable industrial use. Therefore, cocktail also employed hydrolysis wheat bran residue. TLC HPAEC-PAD analyses revealed high conversion rate xylose (91.56 %), placing among most promising biocatalysts saccharification agricultural waste.

Language: Английский

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Bioremediation strategies and mechanisms of bacteria for resistance against heavy metals: a review

Bioremediation Journal, Journal Year: 2024, Volume and Issue: unknown, P. 1 - 33

Published: July 12, 2024

Language: Английский

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Thermophilic lipases in industrial applications: Stutzerimonas stutzeri as a Case Study in Nigeria and the US

GSC Biological and Pharmaceutical Sciences, Journal Year: 2024, Volume and Issue: 27(1), P. 060 - 069

Published: April 6, 2024

Thermophilic lipases derived from Stutzerimonas stutzeri have garnered significant attention in recent years due to their robustness and efficiency various industrial applications. This review delves into the research, development, application of these enzymes, with a comparative analysis between Nigeria United States. In both nations, researchers explored enzymatic properties thermophilic stutzeri, aiming optimize performance for diverse processes. The research encompasses studies on enzyme purification, characterization, genetic engineering enhance catalytic activity stability under extreme conditions. Additionally, efforts been directed towards understanding enzyme's structure-function relationship tailor it specific Nigeria, focus has primarily driven by need sustainable biotechnological solutions industries, including food, pharmaceuticals, biofuel production. enzymes' thermostability makes them particularly suitable high-temperature processes prevalent Nigeria's tropical climate, offering potential cost-effective eco-friendly alternatives conventional chemical catalysts. contrast, States witnessed extensive development applications, strong emphasis biocatalysis pharmaceutical, detergent, sectors. advanced infrastructure investment biotechnology facilitated commercialization lipases, leading integration improve sustainability. Despite similarities objectives, disparities exist technological advancements utilization US. While faces challenges related limited resources infrastructure, US benefits well-established institutions networks, enabling accelerated innovation commercialization. Bridging gaps through international collaborations knowledge exchange could facilitate widespread adoption globally.

Language: Английский

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The Effects of Buffer Nature on Immobilized Lipase Stability Depend on Enzyme Support Loading

Catalysts, Journal Year: 2024, Volume and Issue: 14(2), P. 105 - 105

Published: Jan. 26, 2024

The lipases from Thermomyces lanuginosus (TLL) and Candida antarctica (B) (CALB) were immobilized on octyl-agarose beads at 1 mg/g (a loading under the capacity of support) by overloading support with enzymes. These biocatalysts compared in their stabilities 10 mM sodium phosphate, HEPES, Tris-HCl pH 7. Lowly loaded CALB was more stable than highly preparation, while TLL this effect smaller. Phosphate very negative for stability biocatalyst moderately using both loadings. enzymes HEPES presented a different response as function enzyme (e.g., lowly CALB, similar buffers, but it clearly smaller biocatalysts). Moreover, specific activity versus p-nitrophenol butyrate, triacetin R- or S-methyl mandelate depended buffer, loading, interaction between them. In some cases, almost twice expected could be obtained octyl-CALB, depending buffer. A co-interaction effects specificity buffer nature detected.

Language: Английский

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Characterization of Detergent-Compatible Lipases from Candida albicans and Acremonium sclerotigenum under Solid-State Fermentation

ACS Omega, Journal Year: 2023, Volume and Issue: 8(36), P. 32740 - 32751

Published: Aug. 23, 2023

The purpose of this study was to compare and explore the potential two distinct lipases at industrial levels after their production using wheat bran substrate in solid-state fermentation. Lipases from Candida albicans (C. albicans) Acremonium sclerotigenum (A. sclerotigenum) were characterized assess compatibility suitability for use laundry detergents. effects pH, temperature, metal ions, inhibitors, organic solvents, various commercially available detergents on these studied order activity stability profiles check stain removal ability. Both remained stable across wide pH (7-10) temperature (30-50 °C) ranges. C. lipase exhibited optimum (51.66 U/mL) 7.0 37 °C, while A. showed (52.12 8.0 40 °C. addition Ca2+ Mg2+ ions enhanced activities, sodium dodecyl sulfate (SDS) ethylenediamine tetraacetic acid (EDTA) reduced activities. Lipase both strains tolerance solvents considerable with (>50%); however, performed slightly better. Characterization crude nearly 60% relative incubation 2 h detergents, thus suggesting be employed formulation easy efficient enzyme production. thermostable alkaline makes them an attractive option economic gain by lowering amount detergent used, reducing chemical burden environment.

Language: Английский

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