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|dc.description.abstract||A dual-enzyme process aiming at facilitating the purification of trehalose from maltose isreported in this study. Enzymatic conversion of maltose to trehalose usually leads to thepresence of significant amount of glucose, by-product of the reaction, and unreacted maltose.To facilitate the separation of trehalose from glucose and unreacted maltose, sequential conversionof maltose to glucose and glucose to gluconic acid under the catalysis of glucoamylaseand glucose oxidase, respectively, is studied. This study focuses on the hydrolysis ofmaltose with immobilized glucoamylase on EupergitVR C and CM Sepharose. CM Sepharoseexhibited a higher protein adsorption capacity, 49.35 1.43 mg/g, and was thus selected ascarrier for the immobilization of glucoamylase. The optimal reaction temperature and reactionpH of the immobilized glucoamylase for maltose hydrolysis were identified as 40 C and4.0, respectively. Under such conditions, the unreacted maltose in the product stream of trehalosesynthase-catalyzed reaction was completely converted to glucose within 35 min, withoutdetectable trehalose degradation. The conversion of maltose to glucose could bemaintained at 0.92 even after 80 cycles in repeated-batch operations. It was also demonstratedthat glucose thus generated could be readily oxidized into gluconic acid, which canbe easily separated from trehalose. We thus believe the proposed process of maltose hydrolysiswith immobilized glucoamylase, in conjunction with trehalose synthase-catalyzed isomerizationand glucose oxidase-catalyzed oxidation, is promising for the production andpurification of trehalose on industrial scales.||en_US|
|dc.relation||Biotechnology Progress, Volume29, Issue1, Page(s) 83-90.||en_US|
|dc.title||Enzymatic Processes for the Purification of Trehalose||en_US|
|Appears in Collections:||化學工程學系所|
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