Molecular Aspects of Enzyme Catalysis 1994

DOI: 10.1002/9783527615971.ch6

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Higher Plant Phosphorylases

Katsuyuki Tanizawa

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Cited by 3 publications

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Reaction Engineering Aspects of α-1,4-d-Glucan Phosphorylase Catalysis

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et al. 1997

Biotechnology for Fuels and Chemicals

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Reaction Engineering Aspects of α-1,4-d-Glucan Phosphorylase Catalysis

¹

,

²

,

³

et al. 1997

Biotechnology for Fuels and Chemicals

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Reaction Engineering Aspects of α-l,4-D-Glucan Phosphorylase Catalysis

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et al. 1997

Appl Biochem Biotechnol

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Some important process properties of alpha-l,4-D-glucan phosphorylases isolated from the bacterium Corynebacterium callunae and potato tubers (Solatium tuberosum) were compared. Apart from minor differences in their stability and specificity (represented by the maximum degree of maltodextrin conversion) and a 10-fold higher affinity of the plant phosphorylase for maltodextrin (K (M) of 1.3 g/L at 300 mM of orthophosphate), the performances of both enzymes in a continuous ultrafiltration membrane reactor were almost identical. Product synthesis was carried out over a time course of 300-400 h in the presence or absence of auxiliary pullulanase (increasing the accessibility of the glucan substrate for phosphorolytic attack up to 15-20%). The effect of varied dilution rate and reaction temperature on the resulting productivities was quantitated, and a maximum operational temperature of 40 degrees C was identified.

Maltodextrin Phosphorylase from Escherichia coli: Production and Application for the Synthesis of α‐Glucose‐1‐Phosphatea

et al. 1996

Annals of the New York Academy of Sciences

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