Organic solvent-tolerant, cold-adapted lipases PML and LipS exhibit increased conformational flexibility in polar organic solvents

Dachuri, VinayKumar; Boyineni, Jerusha; Choi, So-Ra; Chung, Hye-Shin; Jang, Sei‐Heon; Lee, ChangWoo

doi:10.1016/j.molcatb.2016.06.003

Cited by 16 publications

(12 citation statements)

References 39 publications

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“…The hNFs of papain were shown to undergo conformational changes, including rearrangement of surface amino acids, stripping of water from the protein surface, and weakening of hydrophobic interactions when exposed to organic solvent. 33 In our experiments, the result of catalysis showed that the hNFs enzyme preparation was organic solventtolerant. Using polar solvents such as DMSO and protic solvents such as ethanol and methanol always lead to higher yields.…”

Section: Effect Of Different Media On 3-benzylidenepentane-24dione Ymentioning

confidence: 62%

Efficient promiscuous Knoevenagel condensation catalyzed by papain confined in Cu₃(PO₄)₂ nanoflowers

Chen

Jiang

et al. 2018

RSC Adv.

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Section: Effect Of Different Media On 3-benzylidenepentane-24dione Ymentioning

confidence: 62%

Efficient promiscuous Knoevenagel condensation catalyzed by papain confined in Cu₃(PO₄)₂ nanoflowers

Chen

Jiang

et al. 2018

RSC Adv.

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“…Some solvents also facilitate the solubility of the substrate, allowing its better interaction with the active site. 32…”

Section: Effect Of Different Compounds On L-asparaginase Activitymentioning

confidence: 99%

Production of L-asparaginase by Aspergillus niveus under solid-state fermentation using agroindustrial byproducts

Amatto

Guimarães

2019

Int J Sci Rep

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Background: L-asparaginase, produced mainly by microrganisms, cleaves L-asparagine to aspartic acid and ammonia as products. This enzyme has been applied in the treatment of the leukemia and in food preparation preventing the acrylamide formation.Methods: Aspergillus niveus was grown in different solid substrates (agroindustrial byproducts) moistened with different agents (tap water, distilled water and several salt solutions) for different periods (24-240 h) at 30ºC. The enzyme extract was obtained with the addition of cold distilled water, agitation at 50 rpm for 30 min and filtration. The filtrate was used to determine the L-asparaginase activity through the hydroximate aspartic methodology using L-asparagine as substrate. The influence of temperature (30-75ºC), pH (3-9) and chemical compounds on the enzyme activity was analyzed. Results: The highest level of enzyme production was obtained using the M1 mixture (wheat bran, crushed soybean, orange peel; 1:1:1, w/w/w) as substrate humidified with Czapeck Dox salt solution (1:0.5, m/v) for 48-120 h, at 30ºC. The best temperature and pH for the enzyme activity were 35ºC and 5.0, respectively. The enzyme activity was increased in the presence of NaCl and some organic solvents (acetonitrile, butanol ethanol, isopropanol and methanol).Conclusions: A. niveus produced L-asparaginase under SSF using a mixture of agroindustrial byproducts as solid substrate in the absence of L-asparagine as inducer. The temperature and pH of activity, as well as the NaCl tolerance, indicate its potential to be applied for different purposes. A. niveus can be an interesting source of L-asparaginase gene to be investigated targeting future application.

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“…Cotton fibers have abundant hydroxyl groups that, like water, benefit stabilization of enzyme proteins [32]. Also the naturally fibrous flexibility of cotton fibers might be beneficial to the enzyme conformation changes usually demanded in catalysis [33]. Besides, the numerous slender filaments of cotton fibers present cotton-PCL with large specific surface and interval volume ( Figure 1b), which help contacts between enzyme molecules and substrates.…”

Section: Stability Of Cotton-pclmentioning

confidence: 99%

A simple room temperature-static bioreactor for effective synthesis of hexyl acetate

Cao

Cong

Kang

et al. 2019

Green Processing and Synthesis

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AbstractFor green synthesis in organic phases, the catalysis of lipases needs to be further improved. Here a strategy is to simulate the activation of lipases at water/oil interface by immobilizing lipase on an available carrier material, which can replace the water at the interface to stabilize enzyme against denaturation from organic phase. The carrier is selected as cotton fiber on which Pseudomonas cepacia lipase is immobilized by physical adsorption in a column glass bottle to form a simple bioreactor together with the bottle. In synthesis of fragrance ester hexyl acetate via transesterification of hexanol with vinyl acetate, the bioreactor exhibits a 3-fold increase in the ability to transform substrate, relative to native lipase in terms of the initial period of reaction at 37°C and 160 rpm. And also the bioreactor is very stable in catalysis for that it has an extra long half life t1/2 = 636 h, calculated from the decrease degree of molar conversions in six times of 6-hour transesterifications. More interestingly, the bioreactor behaves excellent activity at room temperature and in a static state, and can transform nearly 100% hexanol after 48 h. All these indicate that the bioreactor has great potential for industrial application.

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Organic solvent-tolerant, cold-adapted lipases PML and LipS exhibit increased conformational flexibility in polar organic solvents

Cited by 16 publications

References 39 publications

Efficient promiscuous Knoevenagel condensation catalyzed by papain confined in Cu₃(PO₄)₂ nanoflowers

Efficient promiscuous Knoevenagel condensation catalyzed by papain confined in Cu₃(PO₄)₂ nanoflowers

Production of L-asparaginase by Aspergillus niveus under solid-state fermentation using agroindustrial byproducts

A simple room temperature-static bioreactor for effective synthesis of hexyl acetate

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Organic solvent-tolerant, cold-adapted lipases PML and LipS exhibit increased conformational flexibility in polar organic solvents

Cited by 16 publications

References 39 publications

Efficient promiscuous Knoevenagel condensation catalyzed by papain confined in Cu3(PO4)2 nanoflowers

Efficient promiscuous Knoevenagel condensation catalyzed by papain confined in Cu3(PO4)2 nanoflowers

Production of L-asparaginase by Aspergillus niveus under solid-state fermentation using agroindustrial byproducts

A simple room temperature-static bioreactor for effective synthesis of hexyl acetate

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Product

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Efficient promiscuous Knoevenagel condensation catalyzed by papain confined in Cu₃(PO₄)₂ nanoflowers

Efficient promiscuous Knoevenagel condensation catalyzed by papain confined in Cu₃(PO₄)₂ nanoflowers