Kinetic properties of <i>Penicillium cyclopium</i> lipases studied with vinyl esters

Chahinian, Henri; Nini, Lylia; Boitard, Elisabeth; Dubès, J.P.; Sarda, Louis; Comeau, Louis-Claude

doi:10.1007/s11745-000-0601-3

Cited by 23 publications

(18 citation statements)

References 19 publications

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“…The standard deviation was less than 1% of the mean. Cinnamoyl esterase (34), lipase (8), and acetylcholine esterase (7) activities were assayed as previously described.…”

Section: Methodsmentioning

confidence: 99%

Gene Overexpression and Biochemical Characterization of the Biotechnologically Relevant Chlorogenic Acid Hydrolase fromAspergillus niger

Benoit¹,

Asther²,

Bourne

et al. 2007

Appl Environ Microbiol

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The full-length gene that encodes the chlorogenic acid hydrolase from Aspergillus niger CIRM BRFM 131 was cloned by PCR based on the genome of the strain A. niger CBS 513.88. The complete gene consists of 1,715 bp and codes for a deduced protein of 512 amino acids with a molecular mass of 55,264 Da and an acidic pI of 4.6. The gene was successfully cloned and overexpressed in A. niger to yield 1.25 g liter ؊1 , i.e., 330-fold higher than the production of wild-type strain A. niger CIRM BRFM131. The histidine-tagged recombinant ChlE protein was purified to homogeneity via a single chromatography step, and its main biochemical properties were characterized. The molecular size of the protein checked by mass spectroscopy was 74,553 Da, suggesting the presence of glycosylation. ChlE is assembled in a tetrameric form with several acidic isoforms with pIs of around 4.55 and 5.2. Other characteristics, such as optimal pH and temperature, were found to be similar to those determined for the previously characterized chlorogenic acid hydrolase of A. niger CIRM BRFM 131. However, there was a significant temperature stability difference in favor of the recombinant protein. ChlE exhibits a catalytic efficiency of 12.5 ؋ 10 6 M ؊1 s ؊1 toward chlorogenic acid (CGA), and its ability to release caffeic acid from CGA present in agricultural by-products such as apple marc and coffee pulp was clearly demonstrated, confirming the high potential of this enzyme.

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“…The standard deviation was less than 1% of the mean. Cinnamoyl esterase (34), lipase (8), and acetylcholine esterase (7) activities were assayed as previously described.…”

Section: Methodsmentioning

confidence: 99%

Gene Overexpression and Biochemical Characterization of the Biotechnologically Relevant Chlorogenic Acid Hydrolase fromAspergillus niger

Benoit¹,

Asther²,

Bourne

et al. 2007

Appl Environ Microbiol

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“…Thus, the nature of the interface plays an important role in the study of lipolysis (Sarda & Desnuelle, 1958;Egglof et al, 1995;Sayari et al, 2005). Nonlypolytic esterases are defined as enzymes acting on solutions of short chain acyl esters such as ethyl butyrate or vinyl propionate, whereas they poorly hydrolyse long-chain triacylglycerols (Van Tilbeurgh et al, 1993;Chahinian et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

Biochemical and molecular characterization of a lipase produced by Rhizopus oryzae

Salah¹,

Mosbah²,

Fendri³

et al. 2006

FEMS Microbiology Letters

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A novel strain of Rhizopus oryzae WPG secretes a noninduced lipase (ROLw) in the culture medium; purified ROLw is a protein of 29 kDa, the 45 N-terminal amino acid residues were sequenced, this sequence is very homologous to Rhizopus delemar lipase (RDL), Rhizopus niveus lipase (RNL) and R. oryzae lipase (ROL29) sequences; the cloning and sequencing of the part of the gene encoding the mature ROLw, shows two nucleotides differences with RDL, RNL and ROL29 sequences corresponding to the change of the residues 134 and 200; ROLw does not present the interfacial activation phenomenon when using tripropionin or vinyl propionate as substrates; the lipase activity is maximal at pH 8 and at 37 degrees C, specific activities of 3500 or 900 U mg(-1) were measured at 37 degrees C and at pH 8, using olive oil emulsion or tributyrin as substrates, respectively; ROLw is unable to hydrolyse triacylglycerols in the presence of high concentration of bile salts; it is a serine enzyme as it is inhibited by tetrahydrolipstatin and was stable between pH 5 and pH 8.

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“…Hydrolytic activities of soluble and immobilized lipases were assayed using vinyl propionate as substrate, according to the methodology described by Chahinian et al [33]. One international unit of activity was defined as the amount of enzyme that releases 1 μ moL of propionic acid per minute (1 IU) under the assay conditions.…”

Section: Methodsmentioning

confidence: 99%

Immobilization of a Commercial Lipase from Penicillium camembertii (Lipase G) by Different Strategies

et al. 2011

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The objective of this work was to select the most suitable procedure to immobilize lipase from Penicillium camembertii (Lipase G). Different techniques and supports were evaluated, including physical adsorption on hydrophobic supports octyl-agarose, poly(hydroxybutyrate) and Amberlite resin XAD-4; ionic adsorption on the anionic exchange resin MANAE-agarose and covalent attachment on glyoxyl-agarose, MANAE-agarose cross-linked with glutaraldehyde, MANAE-agarose-glutaraldehyde, and epoxy-silica-polyvinyl alcohol composite. Among the tested protocols, the highest hydrolytic activity (128.2 ± 8.10 IU·g−1 of support) was achieved when the lipase was immobilized on epoxy-SiO2-PVA using hexane as coupling medium. Lipase immobilized by ionic adsorption on MANAE-agarose also gave satisfactory result, attaining 55.6 ± 2.60 IU·g−1 of support. In this procedure, the maximum loading of immobilized enzyme was 9.3 mg·g−1 of gel, and the highest activity (68.8 ± 2.70 IU·g−1 of support) was obtained when 20 mg of protein·g−1 was offered. Immobilization carried out in aqueous medium by physical adsorption on hydrophobic supports and covalent attachment on MANAE-agarose-glutaraldehyde and glyoxyl-agarose was shown to be unfeasible for Lipase G. Thermal stability tests revealed that the immobilized derivative on epoxy-SiO2-PVA composite using hexane as coupling medium had a slight higher thermal stability than the free lipase.

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Kinetic properties of Penicillium cyclopium lipases studied with vinyl esters

Cited by 23 publications

References 19 publications

Gene Overexpression and Biochemical Characterization of the Biotechnologically Relevant Chlorogenic Acid Hydrolase fromAspergillus niger

Gene Overexpression and Biochemical Characterization of the Biotechnologically Relevant Chlorogenic Acid Hydrolase fromAspergillus niger

Biochemical and molecular characterization of a lipase produced by Rhizopus oryzae

Immobilization of a Commercial Lipase from Penicillium camembertii (Lipase G) by Different Strategies

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