Maltose Phosphorylase – Catalog Number: B2020187 (1 kU)

Maltose phosphorylase catalyzes the phosphorolysis of maltose to generate glucose-1-phosphate and glucose in the presence of inorganic phosphate (Pi). This listing provides a defined 1 kU fill (Catalog B2020187) supplied as a lyophilized preparation with a listed molecular-weight entry of 220 kDa and storage at −20 °C. The supplier describes use as a molecular tool for various biochemical applications, consistent with the enzyme’s recurring role in carbohydrate-metabolism studies across diverse microorganisms. The concise specification set—amount, supplied form, storage, keyword identity, and biotechnology-grade note—supports straightforward SOP inclusion and inventory traceability for multi-user labs.

In bench workflows, maltose phosphorylase is frequently incorporated when researchers need a controlled source of glucose-1-phosphate or wish to demonstrate phosphorolysis within qualitative teaching modules. The lyophilized format facilitates precise aliquoting and flexible reconstitution into a lab’s preferred buffer system. Because the listing does not prescribe an activity assay format or working concentration, a practical approach is to set up small pilot reactions that vary substrate load, Pi level, pH/ionic strength, and temperature, while documenting incubation times and time-at-temperature during handling. Recording those parameters with lot identifiers helps establish a reproducible operating window and simplifies transfer of conditions between analysts and instruments.

Typical scenarios include assembling qualitative enzyme-panel comparisons for carbohydrate conversion, configuring platform checks where formation of glucose-1-phosphate serves as a readout, and building exploratory cascades in which maltose phosphorolysis is the entry step. When integrating with downstream detection (e.g., colorimetric or chromatographic readouts), it is useful to document any pretreatments of reaction components and to confirm compatibility with the matrix used in your test system. Within research-only boundaries, the clearly documented fields and storage guidance in this offering make maltose phosphorylase a dependable, documentation-friendly component for laboratories standardizing carbohydrate-metabolism–related workflows and instructional exercises.

Why researchers choose this product:

• Listed activity: phosphorolysis of maltose to glucose-1-phosphate and glucose
• Defined 1 kU fill and lyophilized format support precise aliquoting and storage
• Specified storage at −20 °C aligns with routine cold-chain handling
• Documentation-ready fields (amount, molecular-weight entry, storage, keywords, grade) for SOP/LIMS mapping
• Described by the supplier as a molecular tool for diverse biochemical applications

This product is for Research Use Only (RUO). It is not intended for diagnostic or therapeutic use.

References

• 1: Gao Y, Saburi W, Taguchi Y, Mori H. Biochemical characteristics of maltose phosphorylase MalE from Bacillus sp. AHU2001 and chemoenzymatic synthesis of oligosaccharides by the enzyme Biosci Biotechnol Biochem. 2019 Nov;83(11):2097-2109.
• 2: Hüwel S, Haalck L, Conrath N, Spener F. Maltose phosphorylase from Lactobacillus brevis: purification, characterization, and application in a biosensor for ortho-phosphate Enzyme Microb Technol. 1997 Nov 1;21(6):413-20.
• 3: Li G, Wei X, Wu R, Zhou W, Li Y, Zhu Z, You C. Stoichiometric Conversion of Maltose for Biomanufacturing by In Vitro Synthetic Enzymatic Biosystems Biodes Res. 2022 Jul 1;2022:9806749.
• 4: de Kok S, Yilmaz D, Suir E, Pronk JT, Daran JM, van Maris AJ. Increasing free-energy (ATP) conservation in maltose-grown Saccharomyces cerevisiae by expression of a heterologous maltose phosphorylase Metab Eng. 2011 Sep;13(5):518-26.
• 5: Le Breton Y, Pichereau V, Sauvageot N, Auffray Y, Rincé A. Maltose utilization in Enterococcus faecalis J Appl Microbiol. 2005;98(4):806-13.
• 6: Egloff MP, Uppenberg J, Haalck L, van Tilbeurgh H. Crystal structure of maltose phosphorylase from Lactobacillus brevis: unexpected evolutionary relationship with glucoamylases Structure. 2001 Aug;9(8):689-97.
• 7: Nakai H, Petersen BO, Westphal Y, Dilokpimol A, Abou Hachem M, Duus JØ, Schols HA, Svensson B. Rational engineering of Lactobacillus acidophilus NCFM maltose phosphorylase into either trehalose or kojibiose dual specificity phosphorylase Protein Eng Des Sel. 2010 Oct;23(10):781-7.
• 8: Isono N, Yagura S, Yamanaka K, Masuda Y, Mukai K, Katsuzaki H. Enzymatic synthesis of _-d-fructofuranosyl _-d-glucopyranosyl-(1_2)-_-d-glucopyranoside using Escherichia coli glycoside phosphorylase YcjT Biosci Biotechnol Biochem. 2023 Sep 21;87(10):1249-1253.
• 9: Tsumuraya Y, Brewer CF, Hehre EJ. Substrate-induced activation of maltose phosphorylase: interaction with the anomeric hydroxyl group of alpha-maltose and alpha-D-glucose controls the enzyme’s glucosyltransferase activity Arch Biochem Biophys. 1990 Aug 15;281(1):58-65.
• 10: Inoue Y, Yasutake N, Oshima Y, Yamamoto Y, Tomita T, Miyoshi S, Yatake T. Cloning of the maltose phosphorylase gene from Bacillus sp. strain RK-1 and efficient production of the cloned gene and the trehalose phosphorylase gene from Bacillus stearothermophilus SK-1 in Bacillus subtilis Biosci Biotechnol Biochem. 2002 Dec;66(12):2594-9.