Application of a constrained mixture design for lipase production by <i>Penicillium roqueforti</i> ATCC 10110 under solid-state fermentation and using agro-industrial wastes as substrate

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

doi:10.1080/10826068.2021.2004547

Cited by 11 publications

(1 citation statement)

References 43 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Fungi are the preferred source, as they generally produce extracellular enzymes, facilitating the recovery of the enzyme from the fermentation broth [ 15 ]. Lipase-producing fungi are especially found in waste from the vegetable oil and dairy industries, oil-contaminated soils, and spoiled food [ 16 ].…”

Section: Introductionmentioning

confidence: 99%

Purification, Biochemical and Kinetic Characterization of a Novel Alkaline sn-1,3-Regioselective Triacylglycerol Lipase from Penicilliumcrustosum Thom Strain P22 Isolated from Moroccan Olive Mill Wastewater

Hasnaoui

Dab

Mechri

et al. 2022

IJMS

View full text Add to dashboard Cite

A novel extracellular lipase from a filamentous fungus Ascomycota strain, P22, was isolated from olive mill wastewater, then purified and characterized. This strain was identified as Penicillium crustosum Thom based on sequencing analyses. Penicillium crustosum Thom strain P22 lipase (PCrL) was purified 63-fold to homogeneity using ammonium sulfate precipitation and chromatography on a Q-Sepharose Fast Flow column, with a total yield of 34%. The purified PCrL had a molecular mass of 28 kDa, estimated by SDS-PAGE. The 20 NH2-terminal amino-acid residues showed a high degree of homology with those of other Penicillium lipases. The specific activity of PCrL at pH 9 and 37 °C were found to be 5000 and 10,000 U/mg on olive oil and trioctanoin emulsions, respectively. PCrL exhibited clear regioselectivity toward the sn-1 position of the surface-coated triglycerides which were esterified with α-eleostearic acid at the sn-1/3 position. PCrL was completely inhibited by 53 µM of Orlistat, 5 mM of phenylmethylsulfonylfluoride, and 2 mM of diiodopropyl fluorophosphate, suggesting that it belonged to the serine lipase family. PCrL showed high activity and stability in the presence of water-immiscible organic solvents, surfactant, and oxidizing agents, and showed considerable compatibility with commercial laundry detergents. Washing performance analysis revealed that it could effectively remove oil stains. Hence, PCrL has several attractive properties that make it a promising potential candidate for detergent formulations.

show abstract

Section: Introductionmentioning

confidence: 99%