Enzymatic Synthesis of α-Glucose-1-phosphate: A Study Employing a New α-1,4 Glucan Phosphorylase fromCorynebacterium callunae1
作者:
Bernd Nidetzky,
Andreas Weinhäusel,
Richard Grießler,
KlausD. Kulbe,
期刊:
Journal of Carbohydrate Chemistry
(Taylor Available online 1995)
卷期:
Volume 14,
issue 7
页码: 1017-1028
ISSN:0732-8303
年代: 1995
DOI:10.1080/07328309508005393
出版商: Taylor & Francis Group
数据来源: Taylor
摘要:
In synthetic pathways to complex carbohydrates such as oligosaccharides or nucleotide sugars the activated sugar 1-phosphates serve as important starting molecules. In this study the enzymatic synthesis of α-glucose-1-phosphate (Glc-1-P) has been investigated using a new bacterial α-glucan phosphorylase fromCorynebacterium callunae. The major factors governing the rate of reaction and the attainable degree of substrate conversion have been identified and, accordingly, for optimizing the yield and limiting reaction time for the enzymatic process several points must be considered: (i) the pH-dependent equilibrium of reaction, (ii) product inhibition of the phosphorylase and (iii) enzymatic cleavage of α-1,6 glycosidic linkages present in α-1,4-glucans such as starch or maltodextrins by pullulanases to improve their phosphorolytic conversion. Results obtained in continuous experiments with the phosphorylase retained in an ultrafiltration membrane reactor confirmed the complete operational stability of the enzyme for several days at 30 °C. Since no more than approximately 18 % of the inorganic phosphate can be converted into Glc-1-P an efficient procedure for phosphate and product recovery will be particularly important.
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