Activity and stability of a crude lipase from Penicillium aurantiogriseum in aqueous media and organic solvents

Lima, Valéria Marta Gomes de; Krieger, Nádia; Mitchell, David A.; Fontana, José D.

doi:10.1016/s1369-703x(03)00165-7

Cited by 127 publications

(101 citation statements)

References 31 publications

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“…The lipase activity of the fermentation samples was measured by the hydrolysis of p-nitrophenyl palmitate (pNPP) as first described by Winkler and Stuckmann (1979), and modified by Lima et al (2004). One unit of lipase activity is defined as the release of 1 mmol/min of p-nitrophenol (pNP).…”

Section: Lipase Assay and Protein Determinationmentioning

confidence: 99%

Chicken fat and inorganic nitrogen source for lipase production by Fusarium sp. (Gibberella fujikuroi complex)

Oliveira¹,

Lima

2014

Afr. J. Biotechnol.

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In this work, we report the production of lipases by a Fusarium sp. isolate (FCLA-MA41) from Atlantic Forest, using chicken fat and association of organic and inorganic nitrogen sources in submerged fermentation to seek economically attractive bioprocess. A 2-level, 4-factor Central Composite Design (CCD) and response surface methodology (RSM) were used to study the influence of the concentrations of chicken fat, (NH 4 ) 2 SO 4 , Triton X-100 and yeast extract as a nutrient supplement in Vogel minimum salt medium. RSM defined the region with the best response as consisting of the following combination of variables: chicken fat 15.0 mL/L, Triton X-100 15.0 g/L, ammonium sulfate 4.5 g/L and yeast extract 1.0 g/L. A validation study was performed according to the described concentrations and produced an enzymatic activity of 4.22 ± 0.35 U/mL. Considering the cost estimates of the nutrient medium optimized for lipase production, the production cost was $US 518.00/million Units of lipase.

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Section: Lipase Assay and Protein Determinationmentioning

confidence: 99%

Chicken fat and inorganic nitrogen source for lipase production by Fusarium sp. (Gibberella fujikuroi complex)

Oliveira¹,

Lima

2014

Afr. J. Biotechnol.

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“…In the present study, it was observed that Fe+2 and Ca+2 were beneficial for biosynthesis of lipase because these divalent cations stabilize the tertiary structure of enzyme by acting as cofactors, where their presence enhances the catalytic efficiency of the enzyme [37]. It was also observed that enzyme production was least effective when Mn+2 was added in the culture medium.…”

Section: Effect Of Divalent Cationsmentioning

confidence: 57%

Production of an extracellular lipase by Candida utilis NRRL-Y-900 using agro-industrial by-products

Rehman¹,

Rasool²,

Mukhtar³

et al. 2014

Turk J Bioch

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“…8,29,33,51) Surprisingly, the enzyme from C. cladosporioides 194B was stimulated by Mg 2+ (nearly 30% activation), whereas the lipase activities of most microfungi usually remain almost unchanged (or even slightly inhibited) under exposure to Mg 2+ . 53,54) On the other hand, the P. solitum 194A enzyme was highly affected by Pb 2+ , Cu 2+ , and Fe 2+ (about 60% inhibition). Ca 2+ , which has been found to affect fungal lipase activity and stability, 29) had no effect on the activity of these novel lipases.…”

Section: Discussionmentioning

confidence: 99%

Biochemistry of lipolytic enzymes secreted byPenicillium solitumandCladosporium cladosporioides

Chinaglia

Chiarelli

Maggi

et al. 2014

Bioscience, Biotechnology, and Biochemistry

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Two distinct extracellular lipases were obtained from Penicillium solitum 194A, isolated from domestic compost, and Cladosporium cladosporioides 194B, isolated from dairy wastewater. These alkaline enzymes had molecular masses of 42 and 30 kDa, respectively. The P. solitum 194A lipase differed in mass from previously reported enzyme, indicating that it is a novel lipase, and indicating that penicillia can secrete lipase isoenzymes. The C. cladosporioides lipase was more active on esters of medium-chain acids, whereas the P. solitum lipase was more active on longer chained substrates. The C. cladosporioides enzyme displayed higher thermal stability than the P. solitum lipase, preserving full activity up to 48 °C and showing a T50 (10 min) of 60 °C. Their different catalytic properties and good protein stability should make these enzymes suitable for biotechnological applications. Furthermore, the combined use of these two fungal strains may prove to be valuable in lipid-rich waste management.

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Activity and stability of a crude lipase from Penicillium aurantiogriseum in aqueous media and organic solvents

Cited by 127 publications

References 31 publications

Chicken fat and inorganic nitrogen source for lipase production by Fusarium sp. (Gibberella fujikuroi complex)

Chicken fat and inorganic nitrogen source for lipase production by Fusarium sp. (Gibberella fujikuroi complex)

Production of an extracellular lipase by Candida utilis NRRL-Y-900 using agro-industrial by-products

Biochemistry of lipolytic enzymes secreted byPenicillium solitumandCladosporium cladosporioides

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