TN2015000206A1 - Study of a new thermoactive and thermostable alkaline thiol-dependent serine protease serine produced by the strain of Streptomyces koyangensis TN650 having an industrial interest in peptide synthesis and in the formulation of washing detergents. - Google Patents
Study of a new thermoactive and thermostable alkaline thiol-dependent serine protease serine produced by the strain of Streptomyces koyangensis TN650 having an industrial interest in peptide synthesis and in the formulation of washing detergents.Info
- Publication number
- TN2015000206A1 TN2015000206A1 TNP2015000206A TN2015000206A TN2015000206A1 TN 2015000206 A1 TN2015000206 A1 TN 2015000206A1 TN P2015000206 A TNP2015000206 A TN P2015000206A TN 2015000206 A TN2015000206 A TN 2015000206A TN 2015000206 A1 TN2015000206 A1 TN 2015000206A1
- Authority
- TN
- Tunisia
- Prior art keywords
- strain
- enzyme
- thiol
- peptide synthesis
- stap
- Prior art date
Links
Abstract
La présente invention concerne, la purification à homogénéité d'une nouvelle protéase nommée STAP produite à partir de la souche Streptomyces koyangensis TN650 et la caractérisation biochimique de cette enzyme. Cette souche à été nouvellement isolée à partir d'un échantillon pétrolier de Mahres. Les techniques de purification utilisées dans ce travail, ont permis d'aboutir à une solution enzymatique homogène ayant une masse moléculaire de 45125,17 Da déterminée par spectrométrie de masse (MALDI-TOF/MS). Sa pureté a été également vérifiée par le séquençage de son extrémité NH2-terminale (27aa), qui montre une forte homologie avec les protéases à sérine de Streptomyces. L'optimum de l'activité protéase est obtenu à pH 10 et à 70°Csur caséine, cette enzyme demeure pratiquement stable aux pH basiques (7-10) pendant 120 h. Il s'agit d'une enzyme appartenant à la famille des protéases à sérine thiol-dépendante du fait qu'elle est inhibée essentiellement par la PMSF et le DFP, d'une part, et le DTNP,NEM, iodoacéttamide, DTT et 2-ME, d'autre part. Sa thermoactivité et sa thermostabilité sont considérablement améliorées par le calcium à 3 mM. La ST AP se distingue par une large spécificité vis-à-vis des substrats. La ST AP, est une bonne candidate dans la synthèse peptidique car elle montre une bonne activité, stabilité et tolérance en présence de divers solvants organiques à 50% (v/v) en particulier en présence d'isopropanol, de DMF, de chloroforme et du n-heptane. L'enzyme STAP présente également une stabilité remarquable en présence des surfactants (SDS et LAS), des tensioactifs (Tween 20, Tween 80 et Triton X-1 OO), des agents de blanchiments (perborate de sodium et H102) et certains détergents commerciaux liquides et solides (Tide, Nadif et OMO). Ainsi, la STAP semble être intéressante et pourrait être utilisée dans des applications industrielles comme additif biologique dans les détergents liquides et solides, puisqu'elle a un pH optimum d'activité alcalin.The present invention relates to the homogenous purification of a novel protease named STAP produced from the strain Streptomyces koyangensis TN650 and the biochemical characterization of this enzyme. This strain was newly isolated from a petroleum sample of Mahres. The purification techniques used in this work led to a homogeneous enzymatic solution having a molecular mass of 45125.17 Da determined by mass spectrometry (MALDI-TOF / MS). Its purity was also verified by the sequencing of its NH2-terminal end (27aa), which shows strong homology with serine proteases of Streptomyces. The optimum of the protease activity is obtained at pH 10 and at 70 ° C on casein, this enzyme remains practically stable at basic pH (7-10) for 120 h. It is an enzyme belonging to the family of thiol-dependent serine proteases because it is essentially inhibited by PMSF and DFP, on the one hand, and DTNP, NEM, iodoacetamide, DTT and 2 -ME, on the other hand. Its thermoactivity and thermostability are considerably improved by calcium at 3 mM. ST AP is characterized by a high specificity with respect to substrates. ST AP, is a good candidate in peptide synthesis because it shows a good activity, stability and tolerance in the presence of various organic solvents at 50% (v / v), in particular in the presence of isopropanol, DMF, chloroform and n-heptane. The STAP enzyme also has remarkable stability in the presence of surfactants (SDS and LAS), surfactants (Tween 20, Tween 80 and Triton X-1 OO), bleaching agents (sodium perborate and H102) and some commercial detergents liquids and solids (Tide, Nadif and OMO). Thus, STAP appears to be of interest and could be used in industrial applications as a biological additive in liquid and solid detergents, since it has an optimum pH of alkaline activity.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| TNP2015000206A TN2015000206A1 (en) | 2015-05-25 | 2015-05-25 | Study of a new thermoactive and thermostable alkaline thiol-dependent serine protease serine produced by the strain of Streptomyces koyangensis TN650 having an industrial interest in peptide synthesis and in the formulation of washing detergents. |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| TNP2015000206A TN2015000206A1 (en) | 2015-05-25 | 2015-05-25 | Study of a new thermoactive and thermostable alkaline thiol-dependent serine protease serine produced by the strain of Streptomyces koyangensis TN650 having an industrial interest in peptide synthesis and in the formulation of washing detergents. |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| TN2015000206A1 true TN2015000206A1 (en) | 2016-10-03 |
Family
ID=57232740
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| TNP2015000206A TN2015000206A1 (en) | 2015-05-25 | 2015-05-25 | Study of a new thermoactive and thermostable alkaline thiol-dependent serine protease serine produced by the strain of Streptomyces koyangensis TN650 having an industrial interest in peptide synthesis and in the formulation of washing detergents. |
Country Status (1)
| Country | Link |
|---|---|
| TN (1) | TN2015000206A1 (en) |
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2015
- 2015-05-25 TN TNP2015000206A patent/TN2015000206A1/en unknown
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