Immobilization of Glucoamylase Onto Novel Porous Polymer Supports of Vinylene Carbonate and 2-Hydroxyethyl Methacrylate

Abstract

Glucoamylase was immobilized onto novel porous polymer supports. The properties of immobilized glucoamylase and the relationship between the activity of immobilized enzyme and the properties of porous polymer supports were investigated. Compared with the native enzyme, the temperature profile of immobilized glucoamylase was widened, and the optimum pH was also changed. The optimum substrate concentration of immobilized glucoamylase was higher than that of native enzyme. After storage for 23 d, the immobilized glucoamylase still maintained about 84% of its initial activity, whereas the native enzyme only maintained about 58% of the initial activity. Moreover, after using repeatedly seven times, the immobilized enzyme maintained about 85% of its initial activity. Furthermore, the properties of porous polymer supports had an effect on the activity of the immobilized glucoamylase.

Immobilization of Naringinase from Aspergillus Niger on a Magnetic Polysaccharide Carrier

“…The adsorption of pectinase on the epoxy carrier activated by polyethyleneimine was carried out with an efficiency of 12% calculated based on the activity of the enzyme [ 30 ]. The efficiency of immobilization by the adsorption method at the level of a few to several percent is a typical value of this method of immobilization [ 52 , 53 , 54 , 55 , 56 , 57 ]. Significantly higher enzyme immobilization efficiencies, including naringinase, are obtained when using other methods, e.g., gel entrapment [ 28 , 47 , 48 , 54 ].…”

“…The efficiency of immobilization by the adsorption method at the level of a few to several percent is a typical value of this method of immobilization [ 52 , 53 , 54 , 55 , 56 , 57 ]. Significantly higher enzyme immobilization efficiencies, including naringinase, are obtained when using other methods, e.g., gel entrapment [ 28 , 47 , 48 , 54 ]. The efficiency of naringinase immobilization from A. niger CECT 2088 in the polyvinyl alcohol gel was 91.6% calculated based on the total enzyme activity [ 50 ].…”

Carrier free co-immobilization of glucoamylase and pullulanase as combi-cross linked enzyme aggregates (combi-CLEAs)

“…2,3 There are several reports on the immobilization of glucoamylase and pullulanase individually using solid carriers. [4][5][6][7][8][9][10][11] However, only few works report co-immobilization. [12][13][14][15] In these reports, coimmobilized enzymes were found to be more beneficial as they produced larger amounts of glucose by hydrolyzing starch compared with both free enzymes and immobilized enzymes alone.…”

Improved Stabilities of Immobilized Glucoamylase on Functionalized Mesoporous Silica Synthesised using Decane as Swelling Agent

“…Bio-immobilization increases operational stability, easy recovery of products at the end of reaction and storage stability of the enzyme. Glucoamylase effectively immobilized on different supports like porous glass, chitin, polymers [4][5][6], carboxylfunctionalized magnetic nano particles [7][8], bacterial cellulose bead [9], glyoxal agrose [10] and on carbon support sibunit, bulk catalytic filamentous carbon (bulk CFC), activated carbon(AC) [11] and calcined chicken bone particles [12]. Support with appropriate pore diameter is very essential to incorporate the enzyme there should be a perfect match in size between the enzyme and pore structure of the support because enzyme has its own specific size [13].…”