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Thermus thermophilus as a Source of Thermostable Lipolytic Enzymes.

ABSTRACT: Lipolytic enzymes, esterases (EC 3.1.1.1) and lipases (EC 3.1.1.3), catalyze the hydrolysis of ester bonds between alcohols and carboxylic acids, and its formation in organic media. At present, they represent about 20% of commercialized enzymes for industrial use. Lipolytic enzymes from thermophilic microorganisms are preferred for industrial use to their mesophilic counterparts, mainly due to higher thermostability and resistance to several denaturing agents. However, the production at an industrial scale from the native organisms is technically complicated and expensive. The thermophilic bacterium Thermus thermophilus (T. thermophilus) has high levels of lipolytic activity, and its whole genome has been sequenced. One esterase from the T. thermophilus strain HB27 has been widely characterized, both in its native form and in recombinant forms, being expressed in mesophilic microorganisms. Other putative lipases/esterases annotated in the T. thermophilus genome have been explored and will also be reviewed in this paper.

SUBMITTER: Lopez-Lopez O

PROVIDER: S-EPMC5023265 | biostudies-literature | 2015 Nov

REPOSITORIES: biostudies-literature

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Thermus thermophilus as a Source of Thermostable Lipolytic Enzymes.

López-López Olalla O Cerdán María-Esperanza ME González-Siso María-Isabel MI

Microorganisms 20151104 4

Lipolytic enzymes, esterases (EC 3.1.1.1) and lipases (EC 3.1.1.3), catalyze the hydrolysis of ester bonds between alcohols and carboxylic acids, and its formation in organic media. At present, they represent about 20% of commercialized enzymes for industrial use. Lipolytic enzymes from thermophilic microorganisms are preferred for industrial use to their mesophilic counterparts, mainly due to higher thermostability and resistance to several denaturing agents. However, the production at an indus ...[more]

PMID: 27682117

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Project description:Thermal stable ?-glucosidases with transglycosylation activity could be applied to the industrial production of oligosaccharides as well as conjugation of sugars to biologically useful materials. Therefore, ?-glucosidases isolated from thermophiles have gained attention over the past decade. In this study, the characterization of a highly thermostable ?-glucosidase and its thermostability improved mutant from newly isolated strain Thermus thermophilus TC11 were investigated.The recombinant ?-glucosidase (TtAG) from Thermus thermophilus TC11 was expressed in Escherichia coli BL21 (DE3) and purified. The purified enzyme had a molecular mass of 184 kDa and consisted of 59-kDa subunits; it showed hydrolytic activity for pNP-?-D-glucopyranoside (pNPG), sucrose, trehalose, panose, and isomaltooligosaccharides and very low activity for maltose. The highest specific activity of 288.96 U/mg was observed for pNPG at 90 °C and pH 5.0; Pb(2+) provided a 20 % activity increase. TtAG was stable at 70 °C for more than 7 h and had a half-life of 195 min at 80 °C and 130 min at 90 °C. Transglycosylation activity was also observed with sucrose and trehalose as substrates. TtAG showed differences on substrate specificity, transglycosylation, multimerization, effects of metal ions and optimal pH from other reported Thermus ?-glucosidases. One single-substitution TtAG mutant Q10Y with improved thermostability was also obtained from random mutagenesis library. The site-saturation mutagenesis and structural modelling analysis indicated that Q10Y substitution stabilized TtAG structure via additional hydrogen bonding and hydrophobic interactions.Our findings indicate that TtAG is a highly thermostable and more acidic ?-glucosidase distinct from other reported Thermus ?-glucosidases. And this work also provides new insights into the catalytic and thermal tolerance mechanisms of ?-glucosidases, which may guide molecular engineering of ?-glucosidase and other thermostable enzymes for industrial application.

Dataset Information

Thermus thermophilus as a Source of Thermostable Lipolytic Enzymes.

Publications

Thermus thermophilus as a Source of Thermostable Lipolytic Enzymes.

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