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Merck
  • Cicer α-galactosidase immobilization onto functionalized graphene nanosheets using response surface method and its applications.

Cicer α-galactosidase immobilization onto functionalized graphene nanosheets using response surface method and its applications.

Food chemistry (2013-09-05)
Neelesh Singh, Garima Srivastava, Mahe Talat, Himanshu Raghubanshi, Onkar Nath Srivastava, Arvind M Kayastha
摘要

Cicer α-galactosidase was immobilized onto functionalized graphene with immobilization efficiency of 84% using response surface methodology (Box-Behnken design). The immobilized enzyme had higher thermal stability than the soluble one, attractive for industrial applications. Immobilization of the enzyme lowered the Km to 1/3rd compared to the soluble enzyme. Raffinose family oligosaccharides (RFOs) are mainly responsible for flatulence by taking soybean derived food products. The immobilized enzyme can be used effectively for the hydrolysis of RFOs. After ten successive runs, the immobilized enzyme still retained approximately 60% activity, with soybean RFOs. The easy availability of enzyme source, ease of its immobilization on matrices, non-toxicity, increased stability of immobilized enzyme and effective hydrolysis of RFOs increase the Cicer α-galactosidase application in food processing industries.

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产品描述

Sigma-Aldrich
石墨, powder, <20 μm, synthetic
Sigma-Aldrich
石墨, flakes
Sigma-Aldrich
石墨, powder, <45 μm, ≥99.99% trace metals basis
Sigma-Aldrich
α-半乳糖苷 来源于绿咖啡豆, ammonium sulfate suspension, ≥9 units/mg protein
Sigma-Aldrich
石墨, rod, L 150 mm, diam. 3 mm, low density, 99.995% trace metals basis
Sigma-Aldrich
石墨, powder, <150 μm, 99.99% trace metals basis
Sigma-Aldrich
石墨, rod, L 150 mm, diam. 6 mm, 99.995% trace metals basis
Sigma-Aldrich
α-半乳糖苷酶,位置特异性 来源于大肠杆菌, recombinant, expressed in E. coli, buffered aqueous solution