The enzymology services of Creative Enzymes has been recognized world-side due to the meticulous operation processes and the precise results. The integrated test protocol guarantees the rapid turnover and high accuracy. Choosing Creative Enzymes means superior and professional services for enzyme activity measurement. We are proud to provide activity assays for transferases, such as maltose phosphorylase.

Maltose phosphorylase (EC 2.4.1.8) mainly occurs in bacteria, reversibly catalyzes the conversion of maltose and inorganic phosphate into β-D-glucose-1-phosphate and glucose without requiring any cofactors. It is known that maltose phosphorylase is highly specific on maltose and does not react with other disaccharides, whereas in the maltose synthesis direction, β-D-glucosyl fluoride can be used instead of β-D-glucose-1-phosphate. Moreover, arsenate can serve as substitute for phosphate at the cleavage of maltose.

Maltose phosphorylase is of great importance in the analytical determination of phosphate, which related to food and environmental analysis in lakes, standing waters, and especially sewage to prevent eutrophication. Enzymatic assays are based on phosphate-consuming reactions by phosphorylases, one of which is maltose phosphorylase. Nowadays, this enzyme is used in the electrochemical biosensors to achieve rapid detection of nanomolar levels of phosphate in a few minutes. Besides, in other fields of applications, the enzyme is used for the determination of α-amylase activity utilizing the release of maltose. It is also used for the selective detection of maltose in mixtures of oligosaccharides as well as a useful approach to the enzymatic synthesis of trehalose from maltose. Furthermore, monitoring the phosphate level in urine by this enzyme helps detecting possible renal malfunctions and evaluating the bone mineral turnover in humans. Because of multiple promising applications in analysis and health monitoring, maltose phosphorylase is of great studies. Creative Enzymes processes up-to-date experiment methods which can support with efficient and repaid activity assay services for maltose phosphorylase.

Figure: The crystal structure of maltose phosphorylase from Lactobacillus brevis.
Reference: Egloff MP et al. Structure. 2001 9(8): 689-97.

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