Molecular characterization and application of lipase from Bacillus sp. PU1 and investigation of structural changes based on pH and temperature using MD simulation

Esakkiraj, Palanichamy; Antonyraj, Christian Bharathi; Meleppat, Balraj; Ankaiah, Dasari; Ayyanna, Repally; Ahamed, Syed Ibrahim Basheer; Arul, Venkatesan

doi:10.1016/j.ijbiomac.2017.04.111

Cited by 17 publications

(8 citation statements)

References 32 publications

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“…However, lipase activity was inhibited in the presence of 0.1% ( w / v ) SDS, an ionic surfactant, as lipase activity dropped to 21.36% after 30 min of incubation ( Table 4 ). These results were in accordance with the findings by Esakkiraj et al [ 22 ], who revealed that Triton X-100, Tween 80 and Tween 20 enhanced lipase activity from Bacillus sp. PU1 by 33%, 55% and 58%, respectively.…”

Section: Resultssupporting

confidence: 93%

Purification and Characterization of Lipase Produced by Leuconostoc mesenteroides Subsp. mesenteroides ATCC 8293 Using an Aqueous Two-Phase System (ATPS) Composed of Triton X-100 and Maltitol

et al. 2018

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Purification of lipase produced by L. mesenteroides subsp. mesenteroides ATCC 8293 was conducted for the first time using a novel aqueous two-phase system (ATPS) composed of Triton X-100 and maltitol. The partitioning of lipase was optimized according to several parameters including pH, temperature, and crude load. Results showed that lipase preferentially migrated to the Triton X-100 rich phase and optimum lipase partitioning was achieved in ATPS at TLL of 46.4% and crude load of 20% at 30 °C and pH 8, resulting in high lipase purification factor of 17.28 and yield of 94.7%. The purified lipase showed a prominent band on SDS-PAGE with an estimated molecular weight of 50 kDa. The lipase was stable at the temperature range of 30–60 °C and pH range of 6–11, however, it revealed its optimum activity at the temperature of 37 °C and pH 8. Moreover, lipase exhibited enhanced activity in the presence of non-ionic surfactants with increased activity up to 40%. Furthermore, results exhibited that metals ions such as Na+, Mg2+, K+ and Ca2+ stimulated lipase activity. This study demonstrated that this novel system could be potentially used as an alternative to traditional ATPS for the purification and recovery of enzymes since the purified lipase still possesses good process characteristics after undergoing the purification process.

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Section: Resultssupporting

confidence: 93%

Purification and Characterization of Lipase Produced by Leuconostoc mesenteroides Subsp. mesenteroides ATCC 8293 Using an Aqueous Two-Phase System (ATPS) Composed of Triton X-100 and Maltitol

et al. 2018

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“…Lipase produced by Bacillus sp. PU1 at different pH did not present conformational flexibility when exposed at pH 5 and 7, however, at pH 9 there was necessary double of the enzyme for catalysis (Esakkiraj et al, 2017). Medium pH significantly influences the lipase secretion by Thermomyces lanuginosus, and increasing or decreasing pH medium, the lipase activity decreased.…”

Section: Experimental Designmentioning

confidence: 92%

Agroindustrial co-products and waste cooking oil in the production of lipases by thermophilic Bacillus licheniformis SMIA-3

Carvalho¹,

Cruz

Andrade

et al. 2022

Acta Sci Technol

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The present study investigated the potential lipase production for Bacillus licheniformis SMIA-3 using the agro-industrial co-products: orange flour (OF) and grape flour (GF) blend waste cooking oil (WCO). The OF was selected due to its best source for lipase production observed in preliminary tests. Therefore, OF was tested at different fermentation times at 50°C using the statistical design Central Composite Rotatable Design (CCRD) allied to the response surface. An optimal region was found with lipolytic activity of 0.349 U mL-1 with OF and WCO filters around (0.50% w v-1) and between (0.55 and 0.75% w v-1), respectively, and the fermentation time at the central point (42h). Data supplied a method to produce lipase using orange flour and frying oil, as a way to reuse these waste as feedstock to obtain employable lipase and lower production costs with biotechnological applications in industrial sector

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“…In the dPCA method, the dihedral angles (ϕ i , ψ i ) of the studied peptide group were used to perform the calculation of PCA, where i denotes and indexes for the number of peptide group. In dPCA, the free energy surface in terms of two PCs are calculated as:

μ ((),, {normalq}_{1}, {normalq}_{2}) = - k_{B} T \ln P ((),, {normalq}_{1}, {normalq}_{2})

where q 1 and q 2 represent the trajectories along the first two PCs, k B is the Boltzmann's constant, T is the temperature (300 K), and P (q 1 , q 2 ) is the probability distribution calculated by a histogram of the data obtained from MD simulations. All backbone dihedral angles of the P‐loop were calculated from each system at every 1 ps.…”

Section: Methodsmentioning

confidence: 99%

Insight on mutation‐induced resistance to anaplastic lymphoma kinase inhibitor ceritinib from molecular dynamics simulations

Meiler

et al. 2019

Biopolymers

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Ceritinib, an advanced anaplastic lymphoma kinase (ALK) next-generation inhibitor, has been proved excellent antitumor activity in the treatment of ALK-associated cancers. However, the accumulation of acquired resistance mutations compromise the therapeutic efficacy of ceritinib.Despite abundant mutagenesis data, the structural determinants for reduced ceritinib binding in mutants remains elusive. Focusing on the G1123S and F1174C mutations, we applied molecular dynamics (MD) simulations to study possible reasons for drug resistance caused by these mutations. The MD simulations predict that the studied mutations allosterically impact the configurations of the ATP-binding pocket. An important hydrophobic cluster is identified that connects P-loop and the αC-helix, which has effects on stabilizing the conformation of ATP-binding pocket. It is suggested, in this study, that the G1123S and F1174C mutations can induce the conformational change of P-loop thereby causing the reduced ceritinib affinity and causing drug resistance.

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Molecular characterization and application of lipase from Bacillus sp. PU1 and investigation of structural changes based on pH and temperature using MD simulation

Cited by 17 publications

References 32 publications

Purification and Characterization of Lipase Produced by Leuconostoc mesenteroides Subsp. mesenteroides ATCC 8293 Using an Aqueous Two-Phase System (ATPS) Composed of Triton X-100 and Maltitol

Purification and Characterization of Lipase Produced by Leuconostoc mesenteroides Subsp. mesenteroides ATCC 8293 Using an Aqueous Two-Phase System (ATPS) Composed of Triton X-100 and Maltitol

Agroindustrial co-products and waste cooking oil in the production of lipases by thermophilic Bacillus licheniformis SMIA-3

Insight on mutation‐induced resistance to anaplastic lymphoma kinase inhibitor ceritinib from molecular dynamics simulations

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