www.electrophoresis-journal.com Page 1 Electrophoresis Received: 05 22, 2017; Revised: 07 07, 2017; Accepted: 07 25, 2017 This article has been accepted for publication and undergone full peer review but has not been through the copyediting, typesetting, pagination and proofreading process, which may lead to differences between this version and the Version of Record. Please cite this article as doi: 10.1002/elps.201700208 . This article is protected by copyright. All rights reserved. Synthesis of supermacroporous cryogel for bioreactors continuous starch hydrolysis Ederson Paulo Xavier Guilherme a , Jocilane Pereira de Oliveira a , Lorendane Millena de Carvalho b , Igor Viana Brandi a , Sérgio Henrique Sousa Santos a , Gleidson Giordano Pinto de Carvalho c , Junio Cota a , Bruna Mara Aparecida de Carvalho a,* a Institute of Agricultural Sciences, Federal University of Minas Gerais, Montes Claros, MG 39404- 547, Brazil. b Department of Veterinary, Federal University of Viçosa, Viçosa, MG 36570-000, Brazil; c Department of Animal Science, Federal University of Bahia, Salvador, BA 40110-909, Brazil. *Corresponding author. Tel.: +55 021 38 21017915. E-mail address: brunamara.carvalho@gmail.com (B.M.A. Carvalho). Abstract A bioreactor was built by means of immobilizing alpha-amylase from Aspergillus oryzae by encapsulation, through cryopolymerization of acrylamide monomers for the continuous starch hydrolysis. The starch hydrolysis was evaluated regarding pH, the concentration of immobilized amylase on cryogel, the concentration of starch solution and temperature. The maximum value for starch hydrolysis was achieved at pH 5.0, concentration of immobilized enzyme 111.44mg amylase /g criogel , concentration of starch solution 45g/L and temperature of 35ºC. The immobilized enzyme showed a conversion ratio ranging from 68.2 to 97.37%, depending on the pH and temperature employed. Thus, our results suggest that the alpha-amylase from A. oryzae immobilized