Nitin Kumar; Vinay Kumar; Jitendra Sharma
Abstract
The relaxation behavior of gelatin aqueous solutions has been investigated by time resolved dynamic light scattering (TRDLS) measurements at different temperatures spanning the entire sol to gel phase transition behavior of the system (i.e. from 5 min to 1440 min after a sudden quench from high temperature ...
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The relaxation behavior of gelatin aqueous solutions has been investigated by time resolved dynamic light scattering (TRDLS) measurements at different temperatures spanning the entire sol to gel phase transition behavior of the system (i.e. from 5 min to 1440 min after a sudden quench from high temperature sol to low temperature gel state), when the chosen gelatin concentration in water was maintained at 5 % (w/v), well over the overlap threshold. The quantity of interest, structure factor S (q,τ), has been obtained from the experimentally measured autocorrelation function, g2(τ), allowing appropriate heterodyne contribution. The nonlinear regression analysis of the obtained scattering profiles (variation of structure factor vs. delay time) exhibited good fits to the function S(q,τ) ~A exp(-Dq 2 τ) + B exp(-(τ/τc) β ), up tosystem evolution time of 360 min, whereas the data obtained after 360 min showed appropriate fits to S(q,τ) ~A exp(-Dq 2 τ)+ Cτ -α + B exp(-(τ/τc) β ). The temporal behavior of different fit parameters defining the transient structural network formed in the system has been quantified and analyzed under the purview of well-defined theories. Furthermore, the evolution of particle dynamics from fast to slow and then to almost frozen behavior has been explored through the continuous evaluation of ‘Gelation factor (κ)’ at different stages of system evolution times during the measurements.
K. Sangeetha; Y. Yokogawa; E.K. Girija
Abstract
In recent decades bone infection is one of the most challenging issues encountered in biomedical field and local antibiotic delivery is a key strategy to overcome this issue. Hence developing bioactive materials in combination with antibiotics is much focused recently for bone substitutes. Here we report ...
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In recent decades bone infection is one of the most challenging issues encountered in biomedical field and local antibiotic delivery is a key strategy to overcome this issue. Hence developing bioactive materials in combination with antibiotics is much focused recently for bone substitutes. Here we report the fabrication of pristine and natural polymer (gelatin) composite matrices of hydroxyapatite (HA) by a facile wet precipitation method and their drug release behavior from directly loaded and in situ loaded matrices using amoxicillin as the model drug. The products thus obtained were analyzed by X-ray diffraction (XRD), Fourier transform infrared (FT-IR) spectroscopy, thermogravimetry (TG) and scanning electron microscopy (SEM) which confirmed the formation of HA and nanocomposite of HA with gelatin. It was observed that under physiological conditions, for sustained and prolonged release of the drug in situ loading in composite matrix is a favorable approach.
Vandana Singh; Devendra Singh
Abstract
In the present communication, we report on diastase alpha amylase immobilization at guar gum-silica nanohybrid material (H5). The immobilized amylase (H5-Amyl) showed significantly higher bioactivity (21.62 U mg -1 ) as compared to free amylase (15.59 U mg -1 ) in solution at pH 5 and temperature 40°C. ...
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In the present communication, we report on diastase alpha amylase immobilization at guar gum-silica nanohybrid material (H5). The immobilized amylase (H5-Amyl) showed significantly higher bioactivity (21.62 U mg -1 ) as compared to free amylase (15.59 U mg -1 ) in solution at pH 5 and temperature 40°C. The kinetic parameters of the free (Km = 10.66 mg L -1 ; Vmax = 1.36 µmolemL -1 .min -1 ) and the immobilized enzyme (Km = 6.11 mg mL -1 ; Vmax = 1.45 µmolemL -1 .min -1 ) revealed that the immobilization has increased the overall catalytic property of the enzyme. The immobilized enzyme on recycling could show 87% of initial activity even in the sixth cycle. Since immobilization did not hamper the enzymatic reaction rate, the biocatalyst may be suitably exploited in food and pharmaceutical industries.