Screening for Fungi That Have High Lipolytic and Acidolytic Activities in Biomass Support Particles

Miura, Tsunetoshi; Yamané, Tsuneo

doi:10.1271/bbb.61.1252

Cited by 13 publications

(4 citation statements)

References 4 publications

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“…To date, a large number of lipases from bacteria and fungi have been extensively studied, both from the biochemical and from the genetic point of view (3,38,41). The most productive species belongs to genera Geotrichum, Penicillium, Aspergillus and Rhizomucor (30,39). Lipases from unicellular, mainly those produced by various species of genus Pseudomonas, have been proved to be useful both in organic reactions and in the detergent industry (17).…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of extracellular lipase from a new strain: Pseudomonas aeruginosa SRT 9

Borkar¹,

Bodade²,

Rao³

et al. 2009

Braz. J. Microbiol.

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An extra cellular lipase was isolated and purified from the culture broth of Pseudomonas aeruginosa SRT 9 to apparent homogeneity using ammonium sulfate precipitation followed by chromatographic techniques on phenyl Sepharose CL-4B and Mono Q HR 5/5 column, resulting in a purification factor of 98 fold with specific activity of 12307.8 U/mg. The molecular weight of the purified lipase was estimated by SDS-PAGE to be 29 kDa with isoelectric point of 4.5. Maximum lipase activity was observed in a wide range of temperature and pH values with optimum temperature of 55ºC and pH 6.9. The lipase preferably acted on triacylglycerols of long chain (C14-C16) fatty acids. The lipase was inhibited strongly by EDTA suggesting the enzyme might be metalloprotein. SDS and metal ions such as Hg , Ag 2+ and Fe 2+ decreased the lipase activity remarkedly. Its marked stability and activity in organic solvents suggest that this lipase is highly suitable as a biotechnological tool with a variety of applications including organo synthetic reactions and preparation of enantiomerically pure pharmaceuticals. The Km and Vmax value of the purified enzyme for triolein hydrolysis were calculated to be 1.11 mmol/L and 0.05 mmol/L/min respectively.

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Section: Introductionmentioning

confidence: 99%

Purification and characterization of extracellular lipase from a new strain: Pseudomonas aeruginosa SRT 9

Borkar¹,

Bodade²,

Rao³

et al. 2009

Braz. J. Microbiol.

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“…They have been employed in the modification of both fats and oils to provide novel materials of improved characteristics and to upgrade inexpensive raw materials to valuable products by transesterification [7]. To date, a large number of lipases from filamentous fungi have been extensively studied, the most productive species belonging to the genera Geotrichum, Penicillium, Aspergillus and Rhizomucor [8,9]. R. miehei lipase, a 30 kDa monomeric protein [10], features the most of the general characteristics of the lipases and has most often served as a model in order to understand the mechanism of lipases.…”

Section: Introductionmentioning

confidence: 99%

Polyhydric alcohol protective effect on Rhizomucor miehei lipase deactivation enhanced by pressure and temperature treatment

Noël

Lozano

Combes

2005

Bioprocess Biosyst Eng

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The influence of polyhydric alcohols (sorbitol, xylitol, erythritol, glycerol) on the thermal stability of Rhizomucor miehei lipase has been studied at high hydrostatic pressure (up to 500 MPa). In the absence of additives, a protective effect (PE) (the ratio between the residual activities determined at 480 MPa for the enzyme in the presence or absence of polyhydric alcohols) of low-applied pressures (from 50 MPa to 350 MPa) against thermal deactivations (at 50 degrees C and 55 degrees C) has been noticed. In the presence of additives, a strong correlation between PE and the total hydroxyl group concentration has been obtained, for the first time, under treatments of combining denaturing temperatures and high hydrostatic pressures. This relationship does not seem to be dependent on the nature polyhydric alcohols as the same effect could be observed with 1 M sorbitol and 2 M glycerol. This PE, against thermal and high pressure combined lipase deactivation, increases with polyhydric alcohol concentrations, and when temperature increases from 25 degrees C to 55 degrees C.

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“…There have been numerous biochemical and genetic studies on fungal and bacterial lipases until now ( Verger 1984 ; Kirchner et al., 1985 ; Macrae and Hammond, 1985 ). The most important species are Rhizomucor , Aspergillus , Penicillium and Geotrichum involved in lipase production ( Stocklein et al., 1993 ; Miura and Yamane, 1997 ). Lipase enzyme was reported in P. putida ( Lee and Rhee, 1993 ; Jung et al., 2006 ; Fatima et al., 2014 ).…”

Section: Discussionmentioning

confidence: 99%

The main Aflatoxin B1 degrading enzyme in Pseudomonas putida is thermostable lipase

Singh

Mehta

2022

Heliyon

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Screening for Fungi That Have High Lipolytic and Acidolytic Activities in Biomass Support Particles

Cited by 13 publications

References 4 publications

Purification and characterization of extracellular lipase from a new strain: Pseudomonas aeruginosa SRT 9

Purification and characterization of extracellular lipase from a new strain: Pseudomonas aeruginosa SRT 9

Polyhydric alcohol protective effect on Rhizomucor miehei lipase deactivation enhanced by pressure and temperature treatment

The main Aflatoxin B1 degrading enzyme in Pseudomonas putida is thermostable lipase

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