[18] Structure and function of engineered Pseudomonas mendocina lipase

Boston, Matthew; Requadt, C.; Danko, Steve; Jarnagin, Alisha Stephens; Ashizawa, Eunice; Wu, Shan; Poulose, A.J.; Bott, R.

doi:10.1016/s0076-6879(97)84020-7

Cited by 19 publications

(17 citation statements)

References 24 publications

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“…1B). However, the molecular weight of A. Niger lipases A, B and C were 31.57, 30.23 and 32.01 kDa, respectively, which differed from lipase D. The different acid resistances that were evident among lipases A, B, C and D arose as a consequence of genetically determined structural differences (Boston et al 1997). Similar acid resistance was identified by Namboodiri and Chattopadhyaya (2000) for a lipase which was thermostable at pH 5.0-7.5.…”

Section: Results and Discussion Ph Dependencementioning

confidence: 92%

Optimisation of combi‐lipases from Aspergillus niger for the synergistic and efficient hydrolysis of soybean oil

Qiao

Zhang

Guan

et al. 2016

Animal Science Journal

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The enzymatic properties of four lipases (A, B, C and D) from different strains of Aspergillus niger, were investigated, and a 3-factor mixture design and triangular surface analysis were performed to screen the optimal combi-lipase by observing synergistic effects. Lipases B and D differed in optimal pH, temperature and substrate specificity. A combi-lipase with 31.2% lipase B and 68.8% lipase D (w/w, equal to units of 30.36% and 69.64%) exhibited optimal hydrolytic activity on soybean oil, which exceeded the sum of the combined activities of individual lipases (P < 0.05). Free fatty acid from the hydrolyzed soybean oil indicated that the synergistic effect of the combi-lipase resulted from the different fatty acid specificities of the two lipases. Overall, combi-lipase afforded an effective route for the application of lipase enzymes to animal feeds.

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Section: Results and Discussion Ph Dependencementioning

confidence: 92%

Optimisation of combi‐lipases from Aspergillus niger for the synergistic and efficient hydrolysis of soybean oil

Qiao

Zhang

Guan

et al. 2016

Animal Science Journal

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“…In silico Mutagenesis of PML PML is an attractive fat stain remover for industrial applications [22,23]. To check the change in overall structural stability of PML, point mutation was carried out on each residue using ProSA [24,25].…”

Section: Resultsmentioning

confidence: 99%

“…Apart from high activity and stability, alkaline detergentstable lipases should have compatibility with the detergent components in washing conditions including surfactants, oxidants, solvents, and other enzymes [19][20][21]. Pseudomonas mendocina lipase (PML) is such a lipase which has been reported as a potential fat stain remover [22,23]. PML has α/β hydrolase fold with conserved catalytic triad Ser126, His206, and Asp176.…”

Section: Introductionmentioning

confidence: 99%

Emulating structural stability of Pseudomonas mendocina lipase: in silico mutagenesis and molecular dynamics studies

2014

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The need of alkaline detergent-stable lipases has been growing rapidly as they are highly attractive for the production of detergents, biodiesel, pharmaceuticals agents, and various other applications. Lipase from Pseudomonas mendocina (PML) is one such candidate with triglyceride activity and non-homologous with other reported Pseudomonas lipases. The present work provides insights on the role of amino acids toward structural stability of PML. PML was subjected to mutagenesis through in silico point mutations for emulating its structural stability, the foremost property to enhance biophysiochemical properties for industrial process. The structural effects of identified mutants on PML have been analyzed through comparative atomistic molecular dynamics simulations on wild type and mutants. The in silico mutants P187A and P219A were found to stabilize their respective local dynamics and improved the structural stability of PML. The current study sheds light on the rational engineering of PML through in silico methodologies to improvise its structural stability as well as prototype for rational engineering of the lipases.

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“…Lipases (triacylglycerol hydrolases, EC 3.1.1.3) are a diverse class of hydrolytic enzymes specific to a broad variety of acylglycerols and other ester‐linked compounds [1–3]. A large number of lipases have been purified, characterized and crystallized during the last decade [1,4–11].…”

Section: Introductionmentioning

confidence: 99%

Characterization and physicochemical properties of a lipase from Pseudomonas mendocina 3121–1

Surinėnaitė

Bendikienė

Juodka

et al. 2002

Biotech and App Biochem

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The lipase from Pseudomonas mendocina 3121-1 was found to be homogeneous with a molecular mass of 30 kDa by SDS/PAGE. It is composed of two identical subunits. A molecular mass of 62 kDa was determined by gel chromatography on a Toyopearl HW-55F column. Some physicochemical properties of the lipase were investigated using p-nitrophenyl butyrate (p-NPB), Tween 80 solution and Sigma olive-oil emulsion as substrates. The optimum temperature was determined to be 52 degrees C with p-NPB, in the range 50-60 degrees C with Tween 80 and in the range 50-65 degrees C with olive-oil emulsion. The optimum pH was determined to be in the pH range 7.2-7.5, both with Tween and the emulsion, but was unusually alkaline (pH 9.5) with p-NPB. The enzyme was activated for p-NPB hydrolysis by thermal treatment up to 60 min at 60 degrees C, pH 7.0-8.2, but was rapidly inactivated at 70-80 degrees C and at pH 7.0. The lipase was shown to be more thermolabile at 60 degrees C with respect to other two substrates. Using the emulsified substrate, no activity was obtained after preincubating the enzyme for 30 min at 70 degrees C. The enzyme was found to be pH-tolerant when stored at 20 degrees C, pH 6.3-10.3 (100 mM Briton-Robson buffer) as the half-life (t(1/2)) was more than 240 h when p-NPB was used as the substrate. By contrast, the pH-stability range was more narrow (pH 8.0-10.5) with olive-oil emulsion. The effect of various metal ions and EDTA depended on the nature of the substrate.

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[18] Structure and function of engineered Pseudomonas mendocina lipase

Cited by 19 publications

References 24 publications

Optimisation of combi‐lipases from Aspergillus niger for the synergistic and efficient hydrolysis of soybean oil

Optimisation of combi‐lipases from Aspergillus niger for the synergistic and efficient hydrolysis of soybean oil

Emulating structural stability of Pseudomonas mendocina lipase: in silico mutagenesis and molecular dynamics studies

Characterization and physicochemical properties of a lipase from Pseudomonas mendocina 3121–1

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