An organic-solvent-tolerant esterase from turkey pharyngeal tissue

• Published in: Bioresource technology Vol. 101; no. 10; pp. 3732 - 3736
• Main Authors: Cherif, Slim, Gargouri, Youssef
• Format: Journal Article
• Language: English
• Published: Kidlington Elsevier Ltd 01.05.2010; [New York, NY]: Elsevier Ltd; Elsevier
• Subjects: acetone; Animal productions; Animals; beta-mercaptoethanol; Biological and medical sciences; buffers; butanol; Characterization; enzymatic hydrolysis; enzyme activity; enzyme inhibition; Enzyme Stability; enzyme substrates; esterases; Esterases - metabolism; ethanol; Fundamental and applied biological sciences. Psychology; Hydrogen-Ion Concentration; isopropyl alcohol; Meleagris; Meleagris gallopavo; metal ions; methanol; Organic Chemicals - chemistry; Organic solvent; pharynx; Pharynx - enzymology; phenylmethanesulphonyl fluoride; phosphatidylcholines; solvents; Solvents - chemistry; Stability; Temperature; thermal stability; Turkey pharyngeal esterase; Turkeys; Turkey; Characterization; Organic solvent; Turkey pharyngeal esterase; Stability; Farming animal; Enzyme; Poultry; Tolerance; Turkey(bird); Esterases; Pharynx; Vertebrata; Hydrolases; Aves
• ISSN: 0960-8524; 1873-2976
• DOI: 10.1016/j.biortech.2009.12.106

Stability is a crucial factor for the application of enzymes in biotechnology. Investigation of esterase activity in the pharyngeal tissue of turkey ( Meleagris gallopavo), showed that optimum catalytic conditions of pure enzyme were 50 °C and pH 8.5. Turkey pharyngeal esterase (TPE) retained 75% of its maximum activity after incubation for 1 h at 50 °C. Thermostability of the esterase was enhanced in the presence of an analogous substrate: phosphatidylcholine. TPE had a wide pH range of stability (pH 4.0–10.0). Esterase activity was compatible with the presence of organic solvents. Furthermore, the hydrolysis was found to be slightly activated by Ca 2+, but drastically reduced by Zn 2+ and Cu 2+. Phenylmethanesulphonyl fluoride (PMSF) a serine-specific inhibitor, strongly inhibited the esterase activity, whereas β-mercaptoethanol, a thiol group inhibitor, did not show any effect on the activity. Esterase activity in the presence of organic solvents, as well as in acidic and alkaline pHs and at high temperatures makes it a good candidate for its application in non-aqueous biocatalysis.