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含有来自海洋诺卡氏菌属菌株B2的新型α-淀粉酶的结冷胶微球用于固定化。

Gellan gum microspheres containing a novel α-amylase from marine Nocardiopsis sp. strain B2 for immobilization.

作者信息

Chakraborty Samrat, Jana Sougata, Gandhi Arijit, Sen Kalyan Kumar, Zhiang Wang, Kokare Chandrakant

机构信息

Department of Pharmaceutics, Gupta College of Technological Sciences, Asansol 713301, W.B., India.

Department of Pharmaceutics, Gupta College of Technological Sciences, Asansol 713301, W.B., India.

出版信息

Int J Biol Macromol. 2014 Sep;70:292-9. doi: 10.1016/j.ijbiomac.2014.06.046. Epub 2014 Jul 8.

Abstract

A Nocardiopsis sp. stain B2 with an ability to produce stable α-amylase was isolated from marine sediments. The characterization of microorganism was done by biochemical tests and 16S rDNA sequencing. The α-amylase was purified by gel filtration chromatography by using sephadex G-75. The molecular mass of the amylase was found to be 45 kDa by SDS-PAGE and gel filtration chromatography. The isolated α-amylase was immobilized by ionotropic gelation technique using gellan gum (GG). These microspheres were spherical with average particle size of 375.62±21.76 to 492.54±32.18 μm. The entrapment efficiency of these α-amylase loaded GG microspheres was found 74.76±1.32 to 87.64±1.52%. Characterization of α-amylase-gellan gum microspheres was confirmed using FTIR and SEM analysis. The in vitro amylase release kinetic have been studied by various mathematical models that follow the Korsmeyer-Peppas model (R2=0.9804-0.9831) with anomalous (non-Fickian) diffusion release mechanism.

摘要

从海洋沉积物中分离出一株具有产生稳定α-淀粉酶能力的诺卡氏放线菌属菌株B2。通过生化试验和16S rDNA测序对该微生物进行了鉴定。使用葡聚糖G-75通过凝胶过滤色谱法纯化α-淀粉酶。通过SDS-PAGE和凝胶过滤色谱法发现淀粉酶的分子量为45 kDa。使用结冷胶(GG)通过离子凝胶化技术固定分离出的α-淀粉酶。这些微球呈球形,平均粒径为375.62±21.76至492.54±32.18μm。发现这些负载α-淀粉酶的GG微球的包封率为74.76±1.32至87.64±1.52%。使用FTIR和SEM分析对α-淀粉酶-结冷胶微球进行了表征。通过各种遵循Korsmeyer-Peppas模型(R2=0.9804-0.9831)且具有异常(非菲克)扩散释放机制的数学模型研究了体外淀粉酶释放动力学。

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