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1.
Appl Microbiol Biotechnol ; 108(1): 365, 2024 Jun 06.
Artículo en Inglés | MEDLINE | ID: mdl-38842543

RESUMEN

Lipases are important biocatalysts and ubiquitous in plants, animals, and microorganisms. The high growth rates of microorganisms with low production costs have enabled the wide application of microbial lipases in detergent, food, and cosmetic industries. Herein, a novel lipase from Lacticaseibacillus rhamnosus IDCC 3201 (Lac-Rh) was isolated and its activity analyzed under a range of reaction conditions to evaluate its potential industrial application. The isolated Lac-Rh showed a molecular weight of 24 kDa and a maximum activity of 3438.5 ± 1.8 U/mg protein at 60 °C and pH 8. Additionally, Lac-Rh retained activity in alkaline conditions and in 10% v/v concentrations of organic solvents, including glycerol and acetone. Interestingly, after pre-incubation in the presence of multiple commercial detergents, Lac-Rh maintained over 80% of its activity and the stains from cotton were successfully removed under a simulated laundry  setting. Overall, the purified lipase from L. rhamnosus IDCC 3201 has potential for use as a detergent in industrial applications. KEY POINTS: • A novel lipase (Lac-Rh) was isolated from Lacticaseibacillus rhamnosus IDCC 3201 • Purified Lac-Rh exhibited its highest activity at a temperature of 60 °C and a pH of 8, respectively • Lac-Rh remains stable in commercial laundry detergent and enhances washing performance.


Asunto(s)
Detergentes , Estabilidad de Enzimas , Lacticaseibacillus rhamnosus , Lipasa , Lipasa/metabolismo , Lipasa/química , Lipasa/genética , Lacticaseibacillus rhamnosus/enzimología , Lacticaseibacillus rhamnosus/genética , Lacticaseibacillus rhamnosus/química , Concentración de Iones de Hidrógeno , Detergentes/química , Temperatura , Peso Molecular , Proteínas Bacterianas/genética , Proteínas Bacterianas/química , Proteínas Bacterianas/metabolismo
2.
Int J Biol Macromol ; 193(Pt A): 269-275, 2021 Dec 15.
Artículo en Inglés | MEDLINE | ID: mdl-34695495

RESUMEN

Bacterial nanocellulose (BNC) is characterized by high purity and excellent mechanical properties; however, its production is constrained by low yield. Therefore, efforts aimed at improving its yield and material properties are imperative. This study investigated the effect of adding different concentrations (0%, 0.5%, and 1.0%) of cellulose nanocrystal (CNC) in Hestrin-Schramm modified medium on the yield and properties of BNC produced by Komagataeibacter sp. SFCB22-18. The BNC yield increased as following an increase in added CNC concentration. Also, the morphology, structure, crystallinity, thermal stability, and mechanical properties of BNC improved after CNC incorporation. A low CNC concentration (0.1%) favored mechanical strength, whereas 0.5% gave the optimum morphology, structural, and thermal stability. These results showed that modifying BNC with CNC could help increase yield and improve its properties, and thus; the potentiality of BNC in various applications would be much enhanced.


Asunto(s)
Acetobacteraceae/metabolismo , Celulosa/biosíntesis , Nanopartículas/química , Nanoestructuras/química
3.
J Microbiol Biotechnol ; 31(10): 1366-1372, 2021 Oct 28.
Artículo en Inglés | MEDLINE | ID: mdl-34319261

RESUMEN

Bacterial nanocellulose (BNC) is a biocompatible material with a lot of potential. To make BNC commercially feasible, improvements in its production and surface qualities must be made. Here, we investigated the in situ fermentation and generation of BNC by addition of different cellulosic substrates such as Avicel and carboxymethylcellulose (CMC) and using Komagataeibacter sp. SFCB22-18. The addition of cellulosic substrates improved BNC production by a maximum of about 5 times and slightly modified its structural properties. The morphological and structural properties of BNC were investigated by using Fourier transform-infrared spectroscopy (FT-IR), scanning electron microscopy and X-ray diffraction. Furthermore, a type-A cellulose-binding protein derived from Clostridium thermocellum, CtCBD3, was used in a novel biological analytic approach to measure the surface crystallinity of the BNC. Because Avicel and CMC may adhere to microfibrils during BNC synthesis or crystallization, cellulose-binding protein could be a useful tool for identifying the crystalline properties of BNC with high sensitivity.


Asunto(s)
Acetobacteraceae/química , Materiales Biocompatibles/química , Celulosa/química , Nanoestructuras/química , Carboximetilcelulosa de Sodio , Microscopía Electrónica de Rastreo , Unión Proteica , Espectroscopía Infrarroja por Transformada de Fourier , Difracción de Rayos X
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