Quantification of intra- and extra-cellular thermophilic lipase/esterase production by Thermus sp

• Published in: Biotechnology letters Vol. 26; no. 9; pp. 705 - 708
• Main Authors: DOMINGUEZ, A, SANROMAN, A, FUCINOS, P, RUA, M. L, PASTRANA, L, LONGO, M. A
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer 01.05.2004; Springer Nature B.V
• Subjects: Bacteria; Biological and medical sciences; Biotechnology; Biotechnology - methods; Cell Proliferation; Esterases - chemistry; Esters; Fatty Acids - chemistry; Fundamental and applied biological sciences. Psychology; Hydrolysis; Lipase - chemistry; Substrate Specificity; Temperature; Thermus - enzymology; Thermus thermophilus; Thermus thermophilus - enzymology; Time Factors; thermophilic; Thermus; Enzyme; lipase; Triacylglycerol lipase; Thermophily; Esterases; Carboxylic ester hydrolases; extremophiles; Production; Bacteria; Hydrolases; esterase; Quantitative analysis
• ISSN: 0141-5492; 1573-6776
• DOI: 10.1023/B:BILE.0000024092.27943.75

Four Thermus strains produced lipolytic activity when grown in liquid medium for 30 h at 70 degrees C. The highest total lipase/esterase activity (57 U l(-1)) was in Thermus aquaticus YT-1, followed by Thermus thermophilus HB27 and HB8 (33 and 25 U l(-1), respectively), and finally by Thermus sp. (16 U l(-1)). Extra-cellular activity was detected in T. aquaticus YT-1 and T. thermophilus HB27 (33 and 17 U l(-1)). All enzymes were stable at 80 degrees C over 30 min, and their activity towards fatty acid esters increased as substrate chain-length diminished (i.e. hydrolysis rate was up to 6-fold higher on p-nitrophenyl caproate than on laurate).