Optimization of lipase production by <i>Penicillium roqueforti</i> ATCC 10110 through solid-state fermentation using agro-industrial residue based on a univariate analysis

Araujo, Sabryna Couto; Ramos, Marla Rosa Marques Ferreira; Santo, Eliézer Luz do Espírito; Menezes, Luiz Henrique Sales de; Carvalho, Marise Silva de; Tavares, Iasnaia Maria de Carvalho; Franco, Marcelo; Oliveira, Julieta Rangel de

doi:10.1080/10826068.2021.1944203

Cited by 28 publications

(5 citation statements)

References 30 publications

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“…There have been reports of the production of lipases from several different filamentous fungi including Aspergillus niger , Aspergillus oryza , Rhizopus nodosus , Penicillium roquefortii , Penicillium abeanum , Penicillium chrysogenum , Trichoderma lanuginosus , Fusarium oxysporum , Alternaria , etc. [ 70 , 71 , 72 ], and these are the primary sources utilized to produce commercial lipases.…”

Section: Sources Of Microbial Lipasesmentioning

confidence: 99%

The Recent Advances in the Utility of Microbial Lipases: A Review

et al. 2023

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Lipases are versatile biocatalysts and are used in different bioconversion reactions. Microbial lipases are currently attracting a great amount of attention due to the rapid advancement of enzyme technology and its practical application in a variety of industrial processes. The current review provides updated information on the different sources of microbial lipases, such as fungi, bacteria, and yeast, their classical and modern purification techniques, including precipitation and chromatographic separation, the immunopurification technique, the reversed micellar system, aqueous two-phase system (ATPS), aqueous two-phase flotation (ATPF), and the use of microbial lipases in different industries, e.g., the food, textile, leather, cosmetics, paper, and detergent industries. Furthermore, the article provides a critical analysis of lipase-producing microbes, distinguished from the previously published reviews, and illustrates the use of lipases in biosensors, biodiesel production, and tea processing, and their role in bioremediation and racemization.

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Section: Sources Of Microbial Lipasesmentioning

confidence: 99%

The Recent Advances in the Utility of Microbial Lipases: A Review

et al. 2023

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“…Lipolytic enzymes inclusive of lipases enzymes (EC 3.1.1.1, triacylglycerol hydrolases) and the true esterases are considered among the most important of hydrolases enzyme in different applications of biotechnology (Ramnath et al, 2017). Lipases enzyme (triacylglycerol hydrolases, EC 3.1.1.3) in the industry, are a valuable class of enzymes (Araujo et al, 2022) which can catalyze esterification, interesterification, and transesterification reactions in non‐aqueous conditions in addition to their natural role of hydrolyzing triacylglycerol to diacylglycerol, monoacylglycerol as well as glycerol and free fatty acids (Budžaki et al, 2022). These versatile properties enable lipases to be used in a variety of applications, including paper, textiles, food, feed, chemicals, detergents, and medications.…”

Section: Introductionmentioning

confidence: 99%

Heterologous expression and characterization of a novel thermostable and alkali stable recombinant lipase enzyme from Bacillus thuringensis into E. coliBL21(DE3) for detergent formulation

Zafar,

Rahman,

Hamid

et al. 2024

J Surfact & Detergents

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Present study concerned with expression and biochemical characterization of lipase enzyme for potential use in detergent formulation. Lipase gene (1242 bp) of Bacillus thuringensis was cloned and expressed in Escherichia coli BL21 strain using pET‐21a(+) expression vector. Maximum expression of cloned lipase gene was obtained at 37°C with an induction of 0.4 mM IPTG (Isopropyl ß‐D‐1‐thiogalactopyranoside) after 4 h of induction. Recombinant lipase was purified to homogeneity using immobilized metal ion affinity chromatography carrying 109.80 U/mg specific activity with 38.79 purification folds. Molecular mass of purified lipase was determined as 45 kDa using sodium dodecyl sulfate‐polyacrylamide gel electrophoresis. Purified recombinant lipase showed stability up to 90°C and retained significant activity (52%) after 4 h at 90°C. It was also found to be stable at a wide range of pH and in the presence of higher concentrations of several inhibitors (sodium dodecyl sulfate, dimethylsulfoxide, sodium azide, β‐mercaptoethanol, polysorbate 80, dithiothreitol) as well as organic solvents (acetone, methanol, ethanol, isopropanol, n‐butanol). The activity of recombinant lipase was enhanced in the presence of various metal ions and activated up to 200% by Ca2+. The compatibility of recombinant lipase with commercial detergents and other additives as well as its broad substrate specificity endorse the potential application of this enzyme in detergent formulations.

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“…Immobilization of the lipases on traditional supports allows their reuse, but immobilization matrices are often expensive. Costs can be reduced by producing lipases by solid‐state fermentation (SSF) of cheap agricultural materials, drying the solids after the fermentation, and then adding the “dry fermented solids” directly to the reaction medium; this strategy of “natural immobilization” avoids the steps of isolation, purification, and immobilization that are normally required when lipases are produced by submerged fermentation 9–13 …”

Section: Introductionmentioning

confidence: 99%

“…Costs can be reduced by producing lipases by solid-state fermentation (SSF) of cheap agricultural materials, drying the solids after the fermentation, and then adding the "dry fermented solids" directly to the reaction medium; this strategy of "natural immobilization" avoids the steps of isolation, purification, and immobilization that are normally required when lipases are produced by submerged fermentation. [9][10][11][12][13] However, transesterification processes that use dry fermented solids often have long reaction times, leading to low productivities. One strategy that has been used to increase reaction rates in lipase-catalyzed transesterifications is the use of ultrasound (US).…”

Section: Introductionmentioning

confidence: 99%

Transesterification of castor oil catalyzed by a fermented solid produced by Burkholderia contaminans using a bioreactor coupled with ultrasound irradiation

Moreira

Alnoch

Luz

et al. 2022

Biotech and App Biochem

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In this work, ultrasound was used to assist the ethanolysis of castor oil in a solvent-free system, catalyzed by a dry fermented solid containing the lipase from Burkholderia contaminans (BCFS). Reactions were done at 45 • C. The maximum conversion in Erlenmeyer flasks was 71% in 96 h, using a loading of 9% (mass of BCFS in relation to the mass of triacylglycerols in the castor oil) and a molar ratio of ethanol:oil of 6:1, with addition of ethanol in 12 steps. In a packed-bed reactor containing 12 g of BCFS, the conversions were 78% in 48 h, and 83% in 72 h with an ethanol to oil molar ratio of 3:1 and treatment with an ultrasound probe, with maximum power of 500 W, frequency of 20 kHz, and 75% of the maximum power. These results are promising given that, with an ultrasound assisted bioreactor, a higher conversion in a shorter time was achieved, with a lower ethanol to oil molar ratio than was the case in the Erlenmeyer flasks without ultrasound.

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Optimization of lipase production by Penicillium roqueforti ATCC 10110 through solid-state fermentation using agro-industrial residue based on a univariate analysis

Cited by 28 publications

References 30 publications

The Recent Advances in the Utility of Microbial Lipases: A Review

The Recent Advances in the Utility of Microbial Lipases: A Review

Heterologous expression and characterization of a novel thermostable and alkali stable recombinant lipase enzyme from Bacillus thuringensis into E. coliBL21(DE3) for detergent formulation

Transesterification of castor oil catalyzed by a fermented solid produced by Burkholderia contaminans using a bioreactor coupled with ultrasound irradiation

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