Expression and characterization of a cutinase (AnCUT2) from Aspergillus niger

Altammar, Khadijah A.; Omar, Othman; Murad, Abdul Munir Abdul; Bakar, Farah Diba Abu

doi:10.1515/biol-2016-0004

Cited by 6 publications

(2 citation statements)

References 43 publications

(51 reference statements)

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“…The presence of cations in process reaction mixtures can increase or inhibit enzyme activity. Lipase from various sources has shown different degrees of sensitivity to cations and chemical agents (Ahmed Al-Tammar et al 2016). The catalytic activity of An-lipase was not significantly altered by cations except for Fe 3+ , which had a moderate inhibitory effect (Table 2).…”

Section: Biochemical Properties Of An-lipasementioning

confidence: 96%

Synthesis of flavor esters by a novel lipase from Aspergillus niger in a soybean-solvent system

et al. 2019

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To find a lipase for synthesis of flavor esters in food processing, a total of 35 putative lipases from Aspergillus niger F0215 were heterologously expressed and their esterification properties in crude preparations were examined. One of them, named An-lipase with the highest esterification rate (23.1%) was selected for further study. The purified An-lipase had the maximal activity at 20 °C and pH 6.5 and the specific activity of 1293 U/mg. Sixty percent of the activity was maintained in a range of temperatures of 0-30 °C and pHs of 3.0-8.5. The highest hydrolysis activity of An-lipase was towards pNPC (C8), followed by pNPB (C4) and pNPA (C2), then pNPL (C12). K m , V max , k cat, and k cat /K m towards pNPC were 26.7 mmol/L, 129.9 mmol/ (L h), 23.2 s −1 , and 0.8/mM/s, respectively. The ethyl lactate, butyl butyrate, and ethyl caprylate flavor esters were produced by esterification of the corresponding acids with conversion efficiencies of 15.8, 37.5, and 24.7%, respectively, in a soybeanoil-based solvent system. In conclusion, An lipase identified in this study significantly mediated synthesis of predominant flavor esters (ethyl lactate, butyl butyrate, and ethyl caprylate) in a soybean-oil-lacking other toxic organic solvents, which has potential application in food industries.

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Section: Biochemical Properties Of An-lipasementioning

confidence: 96%

Synthesis of flavor esters by a novel lipase from Aspergillus niger in a soybean-solvent system

et al. 2019

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“…The heterologous transformation can be used to make post-translational modifications that increase the stability and activity of the enzyme. By cloning the cutinase AnCUT2 from Aspergillus niger and expressing it in Pichia pastoris Al-Tammar et al [38] verified that the glycosylation of cutinase by P. pastoris increased its molecular mass and modified the value of its isoelectric point allowing the enzyme to be stable over a wide range of pH.…”

Section: Modification Of Cutinasesmentioning

confidence: 99%

Cutinases: Characteristics and Insights in Industrial Production

Martínez

Maicas

2021

Catalysts

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Cutinases (EC 3.1.1.74) are serin esterases that belong to the α/β hydrolases superfamily and present in the Ser-His-Asp catalytic triad. They show characteristics between esterases and lipases. These enzymes hydrolyze esters and triacylglycerols and catalyze esterification and transesterification reactions. Cutinases are synthesize by plant pathogenic fungi, but some bacteria and plants have been found to produce cutinases as well. In nature they facilitate a pathogen’s invasion by hydrolyzing the cuticle that protects plants, but can be also used for saprophytic fungi as a way to nourish themselves. Cutinases can hydrolyze a wide range of substrates like esters, polyesters, triacylglycerols and waxes and that makes this enzyme very attractive for industrial purposes. This work discusses techniques of industrial interest such as immobilization and purification, as well as some of the most important uses of cutinases in industries.

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