Optimization of Alpha-Amylase Production by a Local Bacillus paramycoides Isolate and Immobilization on Chitosan-Loaded Barium Ferrite Nanoparticles
نویسندگان
چکیده
We set out to isolate alpha-amylase producers from soil samples, optimize the production, and immobilize enzyme on chitosan-loaded barium ferrite nanoparticles (CLBFNPs). Alpha-amylase were isolated starch agar plates confirmed by dinitrosalicylic acid assay. The potent was identified phenotypic methods, 16S-rRNA sequencing, phylogenetic mapping. Sequential optimization of ?-amylase production involved use Plackett–Burman (P–BD) central composite designs (CCD), in addition exposing culture different doses gamma irradiation. immobilized CLBFNPs, nanocomposite characterized X-ray diffraction, Fourier-transform infrared spectroscopy, scanning electron microscopy, with energy-dispersive analysis analysis. Forty-five 100 samples. highest activity (177.12 ± 6.12 U/mg) detected MS009 isolate, which as Bacillus paramycoides. increased 222.3 5.07 U/mg when using optimal conditions P–BD CCD, 319.45 4.91 after 6 kGy. Immobilization CLBFNPs resulted higher (246.85 6.76 compared free (222.254 4.89 U/mg), retaining for up five cycles usage. Gamma irradiation improved while immobilization enhanced activity, facilitated recovery, enabled its repetitive use.
منابع مشابه
Bacillus Amyloliquefaciens Alpha-amylase Inhibition by Organic Solvents: A Study on Methanol, Ethanol and Propanol
Alpha-amylase is widely used as an industrial enzyme, and a therapeutic target for which inhibitors are designed. Organic solvents are used to dissolve various compounds that would be studied as moderators of alpha-amylases, but they could themselves affect enzyme activity and stability. Methanol, ethanol and propanol are simple alcohols that may be commonly used to this end, and their effect h...
متن کاملTextural and Structural Characterizations of Mesoporous Chitosan Beads for Immobilization of Alpha-Amylase: Diffusivity and Sustainability of Biocatalyst
In the present study, textural and structural characterizations of chitosan bead for immobilization of alpha amylase were studied in detail by N2 adsorption–desorption, Microspore Analysis (MP), Barrett–Joyner–Halenda (BJH) plots and Field Emission Scanning Electron Microscope (FESEM) observations. Pore structure observation revealed chemical activation of chitosan bead by glutaralde...
متن کاملBiodiesel Production by Aspergillus niger Lipase Immobilized on Barium Ferrite Magnetic Nanoparticles
In this study, Aspergillus niger ADM110 fungi was gamma irradiated to produce lipase enzyme and then immobilized onto magnetic barium ferrite nanoparticles (BFN) for biodiesel production. BFN were prepared by the citrate sol-gel auto-combustion method and characterized by transmission electron microscopy (TEM), X-ray diffraction (XRD), Fourier transform infrared (FTIR) and scanning electron mic...
متن کاملImmobilization of partially purified alpha-amylase enzyme produced by a soil born Bacillus sp
Alpha amylases have various applications in different industries. Immobilization of alpha -amylase produced by a strain of Bacillus sp isolated from soil of Dibrugarh District of Assam, India was studied. Partially purified enzyme with 4062.62U/ml activity was used for immobilization study. 4% Sodium alginate was used for immobilization of enzyme and the optimum temperature, pH and incubation p...
متن کاملSynthesis And Optimization of Streptomycin Loaded Chitosan-Alginate Nanoparticles
Nanoformulation consisting of Streptomycin loaded chitosan-alginate nanoparticles were prepared using ionotropic-pregelation method and optimization was done in terms of polymer concentration, crosslinker concentration and stirring time. The optimal parameters were found to be Chitosan 0.75mg/ml, calcium chloride 1% (w/v) and stirring time 90 min. Polymer (chitosan and sodium-alginate) and cros...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Fermentation
سال: 2022
ISSN: ['2311-5637']
DOI: https://doi.org/10.3390/fermentation8050241