Short communication: energetics of glucoamylase-catalyzed hydrolysis of commercial sago starch

Glucoamylase (EC 3.2.1.3) from Aspergillus niger was used to hydrolyze commercial sago starch into reducing sugars. The energetics of the hydrolysis was studied at optimal substrate concentration, enzyme amount and pH for the process. The ΔH and ΔS estimated via van't Hof analysis were 7.9 J.mo...

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Bibliographic Details
Main Authors: Wee, L.L., Annuar, M.S.B.M., Ibrahim, Shaliza
Format: Article
Language:English
Published: Malaysian Society for Molecular Biology and Biotechnology 2011
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Online Access:http://eprints.um.edu.my/9445/1/Short_communication_Energetics_of_glucoamylase-catalyzed_hydrolysis_of_commercial_sago_starch.pdf
http://eprints.um.edu.my/9445/
http://www.scopus.com/inward/record.url?eid=2-s2.0-84855827473&partnerID=40&md5=0d448000830d4c6671efa60b4dcdfae5 www.msmbb.org.my/apjmbb/html194/194b.pdf
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Summary:Glucoamylase (EC 3.2.1.3) from Aspergillus niger was used to hydrolyze commercial sago starch into reducing sugars. The energetics of the hydrolysis was studied at optimal substrate concentration, enzyme amount and pH for the process. The ΔH and ΔS estimated via van't Hof analysis were 7.9 J.mole -1 and 6.2 J.mole -1.K -1, respectively. The results indicated that the hydrolysis process is an endothermic reaction and spontaneous within the temperature range tested. It is calculated that 26.3 J.mole -1 of activation energy, E a is required for the enzymatic conversion of sago starch into reducing sugars. The spontaneous reaction with relatively low activation energy supported the viability of glucoamylase-catalyzed hydrolysis of sago starch.