| Titre : |
Heterologous expression of alkaline metalloproteinases in bacillus subtilis sck6 for eco-friendly enzymatic unhairing of goatskins |
| Type de document : |
texte imprimé |
| Auteurs : |
Shihao Zhang, Auteur ; Ruoshi Zhang, Auteur ; Xiaoguang Li, Auteur ; Zhe Xu, Auteur ; Yongqiang Tian, Auteur |
| Année de publication : |
2022 |
| Article en page(s) : |
p. 113-123 |
| Note générale : |
Bibliogr. |
| Langues : |
Américain (ame) |
| Catégories : |
Caractérisation
Cuirs et peaux -- Propriétés mécaniques
Cuirs et peaux de chèvres
Epilage enzymatique
Matériaux -- Coloration
Métalloprotéinases
Wet-blue (tannage)Peau tannée au chrome (le chrome donne une couleur bleue)
|
| Index. décimale : |
675 Technologie du cuir et de la fourrure |
| Résumé : |
In this study, alkaline metalloprotease gene 1067 was cloned from Planococcus halotolerans SCU63T and heterologously expressed in Bacillus subtilis SCK6. Using Luria Bertani (LB) broth medium as the initial medium, the optimal medium was obtained through a series of fermentation and culture optimization (g/L): yeast extract (10), soybean powder (15), urea (20), potassium chloride (6.7), calcium chloride (13.3), NaCl (10). On the basis of the optimal medium, the highest enzymatic activity of 1259.21 U/mL could be obtained by culturing at 30°C for 40 h. with pH 8, inoculation amount of 4% and filling amount of 50 mL. EDTA inhibits protease activity and PMSF promotes it, indicating that it was a metalloprotease rather than a serine protease. The optimum reaction temperature of the protease is 70°C, and the optimum pH is 9. The metal ions Zn 2+, Co2+ and surfactant β-ME, Tween 80 can improve the activity of the protease. The results of unhairing, SEM and staining show that this metalloprotease can completely dehair goatskin. Compared with the conventional chemical method, the goatskin after enzymatic unhairing has softer texture and smoother surface, and there is no obvious damage to the goatskin. |
| Note de contenu : |
- MATERIALS AND METHODS : Materials - Construction of recombinant plasmid and expression of 1067 in B. subtilis SCK6 - Optimization of fermentations conditions - Purification of protease 1067 - Enzyme assay - Analysis of enzymatic properties - Unhairing function of protease 1067 - Characterization of protease 1067 unhairing
- RESULTS AND DISCUSSION : Construction of recombinant strain and identification of protease activity - Fermentation optimization - Purification and identification of protease 1067 - Effect of temperature on enzyme activity and stability - Effect of pH on enzyme activity and stability - Effect of metal ions on enzyme activity - Effects of chemicals on enzyme activity - Effect of organic solvents on enzyme activity - Analysis of unhairing - SEM and analysis of tissue staining
- Table 1 : Factors and levels for RSM
- Table 2 : ANOVA for quadratic model
- Table 3 : Effect of metal ions on enzyme activity
- Table 4 : Effect of chemicals on enzyme activity
- Table 5 : Effect of solvents on enzyme activity
- table 6 : Characterization of mechanical properties of wet blue skin |
| DOI : |
https://doi.org/10.34314/jalca.v117i3.4892 |
| En ligne : |
https://drive.google.com/file/d/1z4VjDZxnKDTJf0c5BtRxJKAwUieQ2jK9/view?usp=drive [...] |
| Format de la ressource électronique : |
Pdf |
| Permalink : |
https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=37602 |
in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. CXVII, N° 3 (03/2022) . - p. 113-123
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Heterologous expression of alkaline metalloproteinases in bacillus subtilis sck6 for eco-friendly enzymatic unhairing of goatskins in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXVII, N° 3 (03/2022)
