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1.
J Sci Food Agric ; 104(7): 3883-3893, 2024 May.
Artículo en Inglés | MEDLINE | ID: mdl-38270454

RESUMEN

BACKGROUND: There has been a significant growth in demand for plant-derived protein, and this has been accompanied by an increasing need for sustainable animal-feed options. The aim of this study was to investigate the effect of magnetic field-assisted solid fermentation (MSSF) on the in vitro protein digestibility (IVPD) and functional and structural characteristics of rapeseed meal (RSM) with a mutant strain of Bacillus subtilis. RESULTS: Our investigation demonstrated that the MSSF nitrogen release rate reached 86.3% after 96 h of fermentation. The soluble protein and peptide content in magnetic field feremented rapeseed meal reached 29.34 and 34.49 mg mL-1 after simulated gastric digestion, and the content of soluble protein and peptide in MF-FRSM reached 61.81 and 69.85 mg mL-1 after simulated gastrointestinal digestion, which significantly increased (p > 0.05) compared with the fermented rapeseed meal (FRSM). Studies of different microstructures - using scanning electron microscopy (SEM) and atomic force microscopy (AFM) - and protein secondary structures have shown that the decline in intermolecular or intramolecular cross-linking leads to the relative dispersion of proteins and improves the rate of nitrogen release. The smaller number of disulfide bonds and conformational alterations suggests that the IVPD of RSM was improved. CONCLUSIONS: Magnetic field-assisted solid fermentation can be applied to enhance the nutritional and protein digestibility of FRSM. © 2024 Society of Chemical Industry.


Asunto(s)
Brassica napus , Brassica rapa , Animales , Brassica napus/química , Fermentación , Estructura Molecular , Brassica rapa/metabolismo , Proteínas de Plantas/metabolismo , Péptidos/metabolismo , Nitrógeno/metabolismo , Alimentación Animal/análisis , Digestión , Dieta
2.
Int J Med Mushrooms ; 25(12): 55-64, 2023.
Artículo en Inglés | MEDLINE | ID: mdl-37947064

RESUMEN

This research aimed to use a novel and effective ultrasound (US) approach for obtaining high bio-compound production, hence proposing strategies for boosting active ingredient biosynthesis. Furthermore, the US promotes several physiological effects on the relevant organelles in the cell, morphological effects on the structure of Phellinus igniarius mycelium, and increases the transfer of nutrients and metabolites. One suitable US condition for flavonoid fermentation was determined as once per day for 7-9 days at a frequency 22 + 40 kHz, power density 120 W/L, treated 10 min, treatment off time 7 s. The flavonoid content and production increased about 47.51% and 101.81%, respectively, compared with the untreated fermentation (P < 0.05). SEM showed that sonication changes the morphology and structure of Ph. igniarius mycelium; TEM reveals the ultrasonic treatment causes organelle aggregation. The ultrasound could affect the metabolism of the biosynthesis of the active ingredients.


Asunto(s)
Agaricales , Basidiomycota , Salix , Agaricales/química , Flavonoides/análisis , Fermentación , Basidiomycota/química , Micelio/química
3.
Food Funct ; 13(4): 2306-2322, 2022 Feb 21.
Artículo en Inglés | MEDLINE | ID: mdl-35142318

RESUMEN

Enzymatic hydrolysis-offline and membrane separation (EH-offline MS), enzymatic membrane reactor (EMR) (various operational modes), and conjoined nanofilter-purification (desalination) were used to produce highly stable antihypertensive and antioxidative peptides from ultrasonic-slurry viscosity reduced sea cucumber (A. japonicus) protein. The adoption of the optimum batch parameters by EMR-gradient diafiltration feeding (GDF), water feeding, and substrate feeding ensured a significant (p < 0.05) enhancement in protein conversion degree (PCD) by 60.39, 46.69, and 23.33%, respectively, over the conventional EH-offline MS. Also, the antihypertensive activity (ACE-inhibitory potency) of the peptides produced was in the order EMR-GDF > substrate feeding > water feeding > batch process > EH-offline MS. The EMR-GDF and nanofilter-purification produced highly digestible peptides with ACE-inhibition activities of 79.44% and 77.57% for gastric and gastrointestinal digests, respectively. Peptides with molecular weights of 1000-500 Da and 500 Da significantly contributed to the antihypertensive potency of desalinated peptides. In vitro simulated peptides showed a significant increase in the hydroxyl radical scavenging activity for gastric (77.27%) and gastrointestinal (85.32%) digests. The antioxidative stability of the produced peptides was least affected by high-temperature storage. The high arginine (Arg) and hydrophobic amino acid (HAA) content of the peptides resulted in their improved digestibility. Therefore, conjoined EMR-GDF and nanofilter-purification in the production of highly stable desalinated bioactive peptides for industrial applications could be a viable alternative.


Asunto(s)
Antihipertensivos/farmacología , Antioxidantes/farmacología , Stichopus , Animales , Antihipertensivos/química , Antioxidantes/química , Compuestos de Bifenilo , Pruebas de Enzimas , Filtración , Picratos
4.
Appl Biochem Biotechnol ; 194(4): 1546-1565, 2022 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-34806139

RESUMEN

Keratinase is one of the important proteases, which is widely used for converting keratin of the keratinaceous materials into various value-added products. In this study, a popular keratinase producer, Bacillus licheniformis PWD-1, was exposed to ultraviolet (UV) and He-Ne laser irradiations to develop high keratinase-producing mutants. Laser irradiation showed a higher lethality of cells (94%) than UV treatment (92%), whereas laser treatment required a longer time (75 min) than UV treatment (20 min). A total of 58 mutants were selected from 176 isolates to study protein and keratinase production capability of the mutants. The highest keratin-to-casein (K:C) ratio (1.43) was exhibited by LU11 mutant, which was obtained from the combined laser and UV irradiations. The purified keratinase (65 kDa) of LU11 showed 40% yield 1.7-fold purity, while the respective value for wild enzyme was 29% and 1.3-fold. Both enzymes showed optimal activity at 55 ℃ and pH 8, with a Z value of 15.78 ℃ for LU11 and 19.72 ℃ for wild strain. The Vmax and specific constant (Kcat/Km) of the mutant enzyme were 357.17 U/ml and 33.11 min-1 mM-1, respectively, which were significantly higher than the respective values of wild enzyme (102.04 U/ml and 28.36 min-1 mM-1).


Asunto(s)
Bacillus licheniformis , Bacillus licheniformis/genética , Bacillus licheniformis/metabolismo , Concentración de Iones de Hidrógeno , Queratinas , Mutagénesis , Péptido Hidrolasas/metabolismo
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