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Esterase

About: Esterase is a research topic. Over the lifetime, 7622 publications have been published within this topic receiving 168270 citations.


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Journal ArticleDOI
TL;DR: Carbonic anhydrases belonging to α-CAs showed esterase/phosphatase activity, whereas enzymes belonging to the β-, γ- and ζ-classes were completely devoid of such activity.

49 citations

Journal ArticleDOI
TL;DR: The presence of feruoyl esterase genes present in the genome sequence of the filamentous fungus Neurospora crassa is examined and an orphan gene is identified, the translation of which shows sequence identity with known feruloyl Esterases.
Abstract: Feruloyl esterases constitute an interesting group of enzymes that have the potential for use over a broad range of applications in the agri-food industries. In order to expand the range of available enzymes, we have examined the presence of feruoyl esterase genes present in the genome sequence of the filamentous fungus Neurospora crassa. We have identified an orphan gene (contig 3.544), the translation of which shows sequence identity with known feruloyl esterases. This gene was cloned and the corresponding recombinant protein expressed in Pichia pastoris to confirm that the enzyme (NcFaeD-3.544) exhibits feruloyl esterase activity. Unusually the enzyme was capable of p-coumaric acid release from untreated crude plant cell wall materials. The substrate utilisation preferences of the recombinant enzyme place it in the recently recognised type-D sub-class of feruloyl esterase.

49 citations

Journal ArticleDOI
TL;DR: An esterase that specifically hydrolyzes medium-chain (C(3)-C(5) monoalkyl phthalates was purified from phthalate-grown Micrococcus sp.
Abstract: An esterase that specifically hydrolyzes medium-chain (C(3)-C(5)) monoalkyl phthalates was purified from phthalate-grown Micrococcus sp. YGJ1. The enzyme activity was split into two fractions by hydrophobic chromatography on Phenyl Sepharose, and the enzymes were purified to homogeneity from each fraction. The purified enzymes showed similar properties with respect to molecular mass (60 kDa), subunit molecular mass (27 kDa), N-terminal amino acid sequence, optimal pH (about 7.5), temperature-dependence, substrate specificity, and inhibitor susceptibility. The enzymes showed no activity toward various dialkyl phthalates or aliphatic carboxyl esters. 2-Mercaptoethanol effectively protected the enzymes from spontaneous inactivation. Diethylpyrocarbonate, p-chloromercuribenzoate, Hg(2+), and Cu(2+) strongly inhibited the enzymes, while phenylmethylsulfonyl fluoride produced weak inhibition, and various metal chelating reagents were ineffective. These findings show that the enzymes bear a close resemblance to the putative phthalate ester hydrolase (PehA) of Arthrobacter keyseri 12B.

49 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
202391
2022209
202183
2020112
2019107
2018129