The Identification and Partial Characterization of a Novel Inducible Extracellular Thermostable Esterase from the Archaeon Sulfolobus shibatae

Huddleston, Stuart; Yallop, C.A.; Charalambous, Bambos M.

doi:10.1006/bbrc.1995.2650

Cited by 36 publications

(26 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The adaptation of these microorganisms to extreme habitats is mediated by an interplay between protein folding and hydrolysis (Iida et al 2000, Maupin-Furlow et al 2000, Wadsworth et al 2001. Lipases and esterases from Archaeoglobus fulgidus (Manco et al 2000) and Sulfolobus shibatae (Huddleston et al 1995) have been purified and characterized, and are also of interest in detergent formulations and the dairy industry. Hydrolases and isomerases from extremely halophilic archaea have potential applications in several biotransformations in the production of food supplements; the microorganisms themselves can be exploited in the production of fermented food (Margesin and Schinner 2001).…”

Section: Archaeal Enzymes Of Biotechnological Interestmentioning

confidence: 99%

Perspectives on biotechnological applications of archaea

Schiraldi

Giuliano

Rosa

2002

Archaea

100

View full text Add to dashboard Cite

Summary Many archaea colonize extreme environments. They include hyperthermophiles, sulfur-metabolizing thermophiles, extreme halophiles and methanogens. Because extremophilic microorganisms have unusual properties, they are a potentially valuable resource in the development of novel biotechnological processes. Despite extensive research, however, there are few existing industrial applications of either archaeal biomass or archaeal enzymes. This review summarizes current knowledge about the biotechnological uses of archaea and archaeal enzymes with special attention to potential applications that are the subject of current experimental evaluation. Topics covered include cultivation methods, recent achievements in genomics, which are of key importance for the development of new biotechnological tools, and the application of wild-type biomasses, engineered microorganisms, enzymes and specific metabolites in particular bioprocesses of industrial interest.

show abstract

Section: Archaeal Enzymes Of Biotechnological Interestmentioning

confidence: 99%

Perspectives on biotechnological applications of archaea

Schiraldi

Giuliano

Rosa

2002

Archaea

100

View full text Add to dashboard Cite

show abstract

“…These include esterases from Archaeoglobus fulgidus (31), Sulfolobus solfataricus (33), and Pyrobaculum calidifontis (18). Besides these enzymes, esterases from Sulfolobus acidocaldarius (39,40), Pyrococcus furiosus (21), and Sulfolobus shibatae (19) have been purified and characterized, but their cognate genes have not been reported.…”

mentioning

confidence: 99%

New Thermophilic and Thermostable Esterase with Sequence Similarity to the Hormone-Sensitive Lipase Family, Cloned from a Metagenomic Library

Rhee

Ahn

Kim

et al. 2005

Appl Environ Microbiol

214

134

View full text Add to dashboard Cite

A gene coding for a thermostable esterase was isolated by functional screening of Escherichia coli cells that had been transformed with fosmid environmental DNA libraries constructed with metagenomes from thermal environmental samples. The gene conferring esterase activity on E. coli grown on tributyrin agar was composed of 936 bp, corresponding to 311 amino acid residues with a molecular mass of 34 kDa. The enzyme showed significant amino acid similarity (64%) to the enzyme from a hyperthermophilic archaeon, Pyrobaculum calidifontis. An amino acid sequence comparison with other esterases and lipases revealed that the enzyme should be classified as a new member of the hormone-sensitive lipase family. The recombinant esterase that was overexpressed and purified from E. coli was active above 30°C up to 95°C and had a high thermal stability. It displayed a high degree of activity in a pH range of 5.5 to 7.5, with an optimal pH of approximately 6.0. The best substrate for the enzyme among the p-nitrophenyl esters (C 4 to C 16 ) examined was p-nitrophenyl caproate (C 6 ), and no lipolytic activity was observed with esters containing an acyl chain length of longer than 10 carbon atoms, indicating that the enzyme is an esterase and not a lipase.

show abstract

“…10) In the Sulfolobus species, up to now, two lipolytic enzymes from Sulfolobus acidocdarius have been partially purified and sequenced and one extracellular esterase from Sulfolobus shibate has been isolated. 11,12) The carboxylesterases from Sulfolobus solfataricus P1 and MT4 were also cloned and characterized. 13,14) But the lipolytic enzymes from S. solfataricus P2 have been not reported and their usability as biocatalysts is still unknown.…”

mentioning

confidence: 99%