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Article

Tryptophan phosphorescence study of enzyme flexibility and unfolding in laboratory-evolved thermostable esterases.

Biochemistry - 25 Apr 2000

Gershenson A, Schauerte J A, Giver L, Arnold F H

Abstract excerpt

Directed evolution of p-nitrobenzyl esterase (pNB E) has yielded eight generations of increasingly thermostable variants. The most stable esterase, 8G8, has 13 amino acid substitutions, a melting temperature 17 degrees C higher than the wild-type enzyme, and increased hydrolytic activity toward p-nitrophenyl acetate (pNPA), the substrate used for evolution, at all temperatures. Room-temperature activities of the...

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PMID: 10769121
DOI: 10.1021/bi992473s

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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