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

被引：37

作者：

Chakraborty, Samrat ^{[1
]}

Jana, Sougata ^{[1
]}

Gandhi, Arijit ^{[1
]}

Sen, Kalyan Kumar ^{[1
]}

Zhiang, Wang ^{[2
]}

Kokare, Chandrakant ^{[3
]}

机构：

[1] Gupta Coll Technol Sci, Dept Pharmaceut, Asansol 713301, WB, India

[2] Chinese Acad Sci, Inst Microbiol, Beijing 100080, Peoples R China

[3] Sinhgad Inst Pharm, Dept Pharmaceut, Pune 411041, Maharashtra, India

来源：

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2014年 / 70卷

关键词：

Nocardiopsis sp; alpha-Amylase; Gellan gum; Immobilization; In vitro release; HALOFERAX-MEDITERRANEI; PURIFICATION; NANOPARTICLES; PERSPECTIVE; DELIVERY;

D O I：

10.1016/j.ijbiomac.2014.06.046

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A Nocardiopsis sp. stain B2 with an ability to produce stable a-amylase was isolated from marine sediments. The characterization of microorganism was done by biochemical tests and 16S rDNA sequencing. The alpha-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 SOS-PAGE and gel filtration chromatography. The isolated alpha-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 mu m. The entrapment efficiency of these alpha-amylase loaded GG microspheres was found 74.76 +/- 1.32 to 87.64 +/- 1.52%. Characterization of alpha-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 (R-2 = 0.9804-0.9831) with anomalous (non-Fickian) diffusion release mechanism. (C) 2014 Published by Elsevier B.V.

引用

页码：292 / 299

页数：8

共 28 条

[1] A novel thermostable, acidophilic α-amylase from a new thermophilic "Bacillus sp Ferdowsicous" isolated from Ferdows hot mineral spring in Iran: Purification and biochemical characterization [J].

Asoodeh, Ahmad ;

Chamani, JamshidKhan ;

Lagzian, Milad .

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 2010, 46 (03) :289-297

[2]

BERNFELD P, 1955, ENZYMOLOGY, V1, P149

[3]

Chengyi W.H., 1999, ACTA PHARMACOL SIN, V32, P400

[4] CAN IMMOBILIZATION BE EXPLOITED TO MODIFY ENZYME-ACTIVITY [J].

CLARK, DS .

TRENDS IN BIOTECHNOLOGY, 1994, 12 (11) :439-443

[5] Adaptive response of Haloferax mediterranei to low concentrations of NaCl (<20%) in the growth medium [J].

DSouza, SE ;

Altekar, W ;

DSouza, SF .

ARCHIVES OF MICROBIOLOGY, 1997, 168 (01) :68-71

[6] Organic solvent tolerance of halophilic α-amylase from a Haloarchaeon, Haloarcula sp strain S-1 [J].

Fukushima, T ;

Mizuki, T ;

Echigo, A ;

Inoue, A ;

Usami, R .

EXTREMOPHILES, 2005, 9 (01) :85-89

[7]

Gupta MN, 2002, INDIAN J BIOCHEM BIO, V39, P220

[8] Microbial α-amylases:: a biotechnological perspective [J].

Gupta, R ;

Gigras, P ;

Mohapatra, H ;

Goswami, VK ;

Chauhan, B .

PROCESS BIOCHEMISTRY, 2003, 38 (11) :1599-1616

[9] A PERSPECTIVE ON THE BIOTECHNOLOGICAL POTENTIAL OF EXTREMOPHILES [J].

HERBERT, RA .

TRENDS IN BIOTECHNOLOGY, 1992, 10 (11) :395-402

[10] Carbopol gel containing chitosan-egg albumin nanoparticles for transdermal aceclofenac delivery [J].

Jana, Sougata ;

Manna, Sreejan ;

Nayak, Amit Kumar ;

Sen, Kalyan Kumar ;

Basu, Sanat Kumar .

COLLOIDS AND SURFACES B-BIOINTERFACES, 2014, 114 :36-44

← 1 2 3 →