α-Amylase immobilization on gelatin: Optimization of process variables | Zendy

Nivedita Jaiswal | Zendy; Om Prakash | Zendy; Mahe Talat | Zendy; Syed Hadi Hasan | Zendy; Rajesh K. Pandey | Zendy

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α-Amylase immobilization on gelatin: Optimization of process variables

Author(s) -

Nivedita Jaiswal,

Om Prakash,

Mahe Talat,

Syed Hadi Hasan,

Rajesh K. Pandey

Publication year - 2012

Publication title -

journal of genetic engineering and biotechnology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.729

H-Index - 25

eISSN - 2090-5920

pISSN - 1687-157X

DOI - 10.1016/j.jgeb.2012.03.003

Subject(s) - glutaraldehyde , gelatin , response surface methodology , amylase , chromatography , box–behnken design , chemistry , homogeneous , precipitation , enzyme , biochemistry , mathematics , physics , combinatorics , meteorology

α-Amylase was extracted and purified from soybean seeds to apparent homogeneity by affinity precipitation. The homogeneous enzyme preparation was immobilized on gelatin matrix using glutaraldehyde as an organic hardener. Response surface methodology (RSM) and 3-level-3-factor Box–Behnken design was employed to evaluate the effects of immobilization parameters, such as gelatin concentration, glutaraldehyde concentration and hardening time on the activity of immobilized α-amylase. The results showed that 20% gelatin (w/v), 10% glutaraldehyde (v/v) and 1h hardening time yielded an optimum immobilization of 82.5%

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