Discovery and characterization of a stable lipase with preference toward long-chain fatty acids

Chen, Mei‐Ling; Gao, Xuemin; Yang, Weiren; Sun, Caili; Yang, Junhuan; Zhang, Huaiyuan; Song, Yuanda

doi:10.1007/s10529-019-02765-4

Cited by 3 publications

(3 citation statements)

References 32 publications

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“…Thus, the reduction in NO15G02830 transcription associated with reduced 6mA modification may explain the reduction in lipids. NO05G00120 encodes a lipase, which hydrolyzes the ester bonds of lipids with a substrate preference ( Long et al., 1998 ; Chen et al., 2020 ; Jithu Paul, 2020 ). Among the ∼40 candidate lipase genes in N .…”

Section: Resultsmentioning

confidence: 99%

Genome-wide adenine N6-methylation map reveals epigenomic regulation of lipid accumulation in Nannochloropsis

Gong,

Wang,

Wei

et al. 2024

Plant Communications

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Section: Resultsmentioning

confidence: 99%

Genome-wide adenine N6-methylation map reveals epigenomic regulation of lipid accumulation in Nannochloropsis

Gong,

Wang,

Wei

et al. 2024

Plant Communications

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“…This is the case when the nourishing value of triacylglycerols is the key point, as this property depends not only on the fatty acid composition, but also on their positional distribution. Therefore, lipases can be very useful for the preparation of novel structured lipids, possessing improved dietary or functional properties, such as low-caloric triglycerides [199], or for the enrichment of triglycerides with ω-3 poly-unsaturated fatty acids, such as eicosapentaenoic acid or docosahexaenoic acid [198,[200][201][202].…”

Section: Oils and Fats As Heterogeneous Substratesmentioning

confidence: 99%

One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates

et al. 2020

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Lipases are among the most utilized enzymes in biocatalysis. In many instances, the main reason for their use is their high specificity or selectivity. However, when full modification of a multifunctional and heterogeneous substrate is pursued, enzyme selectivity and specificity become a problem. This is the case of hydrolysis of oils and fats to produce free fatty acids or their alcoholysis to produce biodiesel, which can be considered cascade reactions. In these cases, to the original heterogeneity of the substrate, the presence of intermediate products, such as diglycerides or monoglycerides, can be an additional drawback. Using these heterogeneous substrates, enzyme specificity can promote that some substrates (initial substrates or intermediate products) may not be recognized as such (in the worst case scenario they may be acting as inhibitors) by the enzyme, causing yields and reaction rates to drop. To solve this situation, a mixture of lipases with different specificity, selectivity and differently affected by the reaction conditions can offer much better results than the use of a single lipase exhibiting a very high initial activity or even the best global reaction course. This mixture of lipases from different sources has been called “combilipases” and is becoming increasingly popular. They include the use of liquid lipase formulations or immobilized lipases. In some instances, the lipases have been coimmobilized. Some discussion is offered regarding the problems that this coimmobilization may give rise to, and some strategies to solve some of these problems are proposed. The use of combilipases in the future may be extended to other processes and enzymes.

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“…synthesis, environment, detergents, pharmaceutical, and cosmetics production etc. (Casas-Godoy et al 2018;Chen et al 2020). Oleates synthesis mediated by lipases is a research hotspot in recent years, because that oleates can be used in various industrial, including biodiesel, emulsifying agents and emollient esters (Khan et al 2015;Mayilvahanan et al 2019;Yan et al 2016).…”

Section: Introductionmentioning

confidence: 99%

Heterologous expression and biochemical characterization of a cold-active lipase from Rhizopus microsporus suitable for oleate synthesis and bread making

et al. 2021

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Objectives Cold-active lipases which show high specific activity at low temperatures are attractive in industrial applications in terms of product stability and energy saving. We aimed to identify novel cold-active lipase suitable for oleates synthesis and bread making. Results A novel lipase gene (RmLipA) from Rhizopus microsporus was cloned and heterologously expressed in Pichia pastoris. The encoding sequence displayed 75% identity to the lipase from R. niveus. The highest extracellular lipase activity of 7931 U/mL was achieved in a 5-L fermentation. The recombinant enzyme (RmLipA) was optimally active at pH 8.0 and 20-25 °C, respectively, and stable over a wide pH range of 2.0-11.0. The enzyme was a cold-active lipase, exhibiting [ 80% of its maximal activity at 0 °C. RmLipA was a sn-1,3 regioselective lipase, and preferred to hydrolyze pNP esters and triglycerides with relatively long chain fatty acids. RmLipA synthesized various oleates using oleic acid and different alcohols as substrates ([ 95%). Moreover, it significantly improved the quality of bread by increasing its specific volume (21.7%) and decreasing its crumb firmness (28.6%). Conclusions A novel cold-active lipase gene from R. microsporus was identified, and its application potentials were evaluated. RmLipA should be a potential candidate in oleates synthesis and bread making industries.

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Discovery and characterization of a stable lipase with preference toward long-chain fatty acids

Cited by 3 publications

References 32 publications

Genome-wide adenine N6-methylation map reveals epigenomic regulation of lipid accumulation in Nannochloropsis

Genome-wide adenine N6-methylation map reveals epigenomic regulation of lipid accumulation in Nannochloropsis

One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates

Heterologous expression and biochemical characterization of a cold-active lipase from Rhizopus microsporus suitable for oleate synthesis and bread making

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