Title: Substrate Specificity of Maltotetraose-forming Amylase from an Alcaligenes sp.
Abstract: A maltotetraoae - forming amylase from Alcaligenes sp. hydrolyzed only the a1, 4-glucosidic linkages of maltooligosaccharides, starch or glycogen. The product of starch glycogen hydrolyzed by G4 A was G4; Hydrolysis products of G5, G6,and G7 were G4 + G, G4 + G2 and G4+G3 respectively, and their rate of hydrolysis was G5G6G7. The degree of hydrolysis of amylose was 100%, that of various starch, 60 ̄74%, while that of glycogen only 34%. It was concluded that G4A was an exo-amylase which cleaved the fourth bond from the non-reducing end of maltooligosaccharides, starch or glycogen. The Km values of G4A for G5, G6, G 7and amylose, soluble starch, glutinous rice starch, amylopectin, glycogen, dextrin were l.156, 0.926, 0.877 mM and 3.28, 3.2, 3.1, 2.8, 2.42, 3 .29 mg/ml respectively; The Vmax values of G4A for the above substrates were 1961, 15385, 17857 and 43990, 29822, 29362, 23582, 14615, 32020 mgG4·h-1·mg-1 respectively.
Publication Year: 1995
Publication Date: 1995-01-01
Language: en
Type: article
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