Ferulic acid esterase‐III from Aspergillus niger does not exhibit lipase activity

Aliwan, Fraj O; Kroon, Paul A.; Faulds, Craig B.; Pickersgill, Richard W.; Williamson, Gary

doi:10.1002/(sici)1097-0010(19990301)79:3<457::aid-jsfa283>3.3.co;2-7

Cited by 12 publications

(16 citation statements)

References 4 publications

(5 reference statements)

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“…The distinct structural difference between the two enzymes correlates well with their respective enzymatic properties, i.e., esterases are active on water‐soluble esters and show no lipase activity , whereas the opposite is true for TLL. The crystal structure of TLL grown at low ionic strength and in the presence of mixed micelles of didodecyl phosphatidyl choline shows a conformational change toward an open lid resembling that of FAEA (PDB entry, 1EIN , gray cartoon (Fig.…”

Section: Changing the Activation Mechanism In Tll By Rational Designmentioning

confidence: 83%

Understanding the activation mechanism of Thermomyces lanuginosus lipase using rational design and tryptophan‐induced fluorescence quenching

Skjold-Jørgensen

Vind

Svendsen

et al. 2016

Euro J Lipid Sci & Tech

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The attractiveness of lipases as industrial biocatalysts underlines the importance of understanding their molecular action in detail, helping future efforts to improve performance and applicability. Lipases represent a special class of carboxyl ester hydrolases, which act on long‐chained water insoluble acyl‐glycerols at the water‐lipid interface. This heterogeneous catalysis makes it very difficult to monitor the structural changes taking place in the enzyme during activation in its preferred milieu. In this review, we cover recent developments toward a deeper understanding of the interfacial activation phenomenon of lipases and discuss a selection of biophysical methods suitable for studying lipase activation. For many lipases, such as that from Thermomyces lanuginosus, a structural domain called the “lid” is directly involved in the activation process. This has been shown through alteration of the lid‐residue composition using rational design. The resulting lid‐mutants have highlighted the lid's role in governing enzymatic activity and interfacial activation. Moreover, a recently developed fluorescence‐based technique called the Tryptophan Induced Quenching method has proved to enable the direct measurement of lipase activation in water‐ethanol mixtures, and thus represents an intriguing method to gain further insight into the structural movements taking place at the water‐lipid interface. Practical applications: Lipases are important industrial biocatalysts widely used in industrial applications including detergent, leather, paper, fuel, fine chemicals, baking, cosmetics, and food. Knowledge of structural changes of lipase upon activation and identification of the amino acids involved in lipase activation is crucial for design of new variants with improved or new properties. Rational design of the lid‐region in lipases has an interesting potential for optimization of lipase function and adapting them to different environments. In order to leverage on the design of new lipase variants and their altered function, methods that enable direct measurement of lipase action directly in solution, in real time, are desired. In this context, fluorescence based methods have shown great potential and provides interesting perspectives for probing the delicate movements occurring in lipases upon activation. Interfacial activation of lipases and the lid movements studied by rational design, fluorescence quenching methods, and solvent effect – polarity driven activation.

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Section: Changing the Activation Mechanism In Tll By Rational Designmentioning

confidence: 83%

Understanding the activation mechanism of Thermomyces lanuginosus lipase using rational design and tryptophan‐induced fluorescence quenching

Skjold-Jørgensen

Vind

Svendsen

et al. 2016

Euro J Lipid Sci & Tech

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“…Like the prototype type A FAE, represented by Aspergillus niger FAEA, TtFAE exhibited weak or insignificant lipase activity (Aliwan et al 1999). In Levasseur et al (2006) and Vieites et al (2010).…”

Section: Discussionmentioning

confidence: 96%

Thermostable feruloyl esterase for the bioproduction of ferulic acid from triticale bran

Abokitse

Bergeron

et al. 2010

Appl Microbiol Biotechnol

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“…The spacing between these residues in the amino acid sequences of lipases is conserved and is also present in FaeA, suggesting a similar active site for this enzyme. No lipase activity could be detected for FaeA (9).…”

Section: Accessory Enzymes Involved In the Degradation Of Plant Cell mentioning

confidence: 99%

AspergillusEnzymes Involved in Degradation of Plant Cell Wall Polysaccharides

Vries

Visser

2001

Microbiol Mol Biol Rev

879

585

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SUMMARY Degradation of plant cell wall polysaccharides is of major importance in the food and feed, beverage, textile, and paper and pulp industries, as well as in several other industrial production processes. Enzymatic degradation of these polymers has received attention for many years and is becoming a more and more attractive alternative to chemical and mechanical processes. Over the past 15 years, much progress has been made in elucidating the structural characteristics of these polysaccharides and in characterizing the enzymes involved in their degradation and the genes of biotechnologically relevant microorganisms encoding these enzymes. The members of the fungal genus Aspergillus are commonly used for the production of polysaccharide-degrading enzymes. This genus produces a wide spectrum of cell wall-degrading enzymes, allowing not only complete degradation of the polysaccharides but also tailored modifications by using specific enzymes purified from these fungi. This review summarizes our current knowledge of the cell wall polysaccharide-degrading enzymes from aspergilli and the genes by which they are encoded.

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Ferulic acid esterase‐III from Aspergillus niger does not exhibit lipase activity

Cited by 12 publications

References 4 publications

Understanding the activation mechanism of Thermomyces lanuginosus lipase using rational design and tryptophan‐induced fluorescence quenching

Understanding the activation mechanism of Thermomyces lanuginosus lipase using rational design and tryptophan‐induced fluorescence quenching

Thermostable feruloyl esterase for the bioproduction of ferulic acid from triticale bran

AspergillusEnzymes Involved in Degradation of Plant Cell Wall Polysaccharides

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