2004Starch - StärkeRequires access

A more Efficient Starch Degradation by the Combination of Hydrolase and Transferase Activities of α‐Amylase and Cyclomaltodextrin Glucanotransferase

Alina Moreno, Gloria Saab‐Rincón, Rosa I. Santamaría, Xavier Soberón, Agustı́n López-Munguı́a

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Abstract

Abstract α‐Amylases catalyze the hydrolysis of internal α‐(1→4) linkages of glucose polymers as their main reaction; however, some α‐amylases catalyze transfer reactions in addition to hydrolysis. It has been observed that those α‐amylases capable of transferring glycoside residues are also those that generate low molecular weight products from their action on starch (i.e. saccharifying α‐amylases). In this paper the product profiles of a liquefying α‐amylase, a cyclomaltodextrin glucanotransferase and both enzymes acting together on starch and maltodextrins are compared. The increase in glucose and maltose concentration, when both enzymes act together, is due to the combined action of the transfer and hydrolytic activity of CGTase and the liquefying α‐amylase, respectively.

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Abstract α‐Amylases catalyze the hydrolysis of internal α‐(1→4) linkages of glucose polymers as their main reaction; however, some α‐amylases catalyze transfer reactions in addition to hydrolysis. It has been observed that those α‐amylases capable of transferring glycoside residues are also those that generate low molecular weight products from their action on starch (i.e. saccharifying α‐amylases). In this paper the product profiles of a liquefying α‐amylase, a cyclomaltodextrin glucanotransferase and both enzymes acting together on starch and maltodextrins are compared. The increase in glucose and maltose concentration, when both enzymes act together, is due to the combined action of the transfer and hydrolytic activity of CGTase and the liquefying α‐amylase, respectively.

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Available abstract

Abstract α‐Amylases catalyze the hydrolysis of internal α‐(1→4) linkages of glucose polymers as their main reaction; however, some α‐amylases catalyze transfer reactions in addition to hydrolysis. It has been observed that those α‐amylases capable of transferring glycoside residues are also those that generate low molecular weight products from their action on starch (i.e. saccharifying α‐amylases). In this paper the product profiles of a liquefying α‐amylase, a cyclomaltodextrin glucanotransferase and both enzymes acting together on starch and maltodextrins are compared. The increase in glucose and maltose concentration, when both enzymes act together, is due to the combined action of the transfer and hydrolytic activity of CGTase and the liquefying α‐amylase, respectively.

Key concepts: Maltose, Hydrolysis, Amylase, Starch, Glycoside hydrolase, Chemistry, Glycoside, Enzyme

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A more Efficient Starch Degradation by the Combination of Hydrolase and Transferase Activities of α‐Amylase and Cyclomaltodextrin Glucanotransferase — Research Paper | ScholarLens