Enzyme Activity Measurement for Glucan 1,4-Alpha-Maltohexaosidase

With the decades of experiences and advanced technologies, Creative Enzymes prides itself on commitment to providing customers with products and services of the highest quality. Creative Enzymes is a global leader in the field of enzyme activity assays. We are proud to offer the most reliable enzyme activity quantitation for glucan 1,4-alpha-maltohexaosidase.

Some bacterial α-amylases dominantly produce maltotetraose (G4), maltopentaose (G5), or maltohexaose (G6) from starch and related α-1,4-glucans, while most α-amylases further convert them to glucose and/or maltose as final products. Since such maltooligosaccharides are useful for their low sweetness, low viscosity, high moisturizing effect, and high efficiency for digestion and absorption, these enzymes have been important in the food and pharmaceutical industries. The reaction mechanism of the enzymes producing particular oligosaccharides is distinct from that of usual α-amylases. Their important properties are presumed to have four, five, or six subsites from the active center to produce the particular oligosaccharides and to prevent them from further degradation. Glucan 1,4-alpha-maltohexaosidase (EC 3.2.1.98; 4-alpha-D-glucan maltohexaohydrolase; G6-amylase) from alkalophilic Bacillus sp.707, which belongs to glycoside hydrolase family 13, produces G6 from starch and related α-1,4-glucans in the yield of >30% of the total products from short-chain amylose (DP = 17). Glucan 1,4-alpha-maltohexaosidase was discovered in 1971 by Kainuma et al. as a cell-bound enzyme and shown to be the fourth exo-amylase. The amino acid sequence of glucan 1,4-alpha-maltohexaosidase is 65.5%, 65.9%, and 66.3% identical to those of liquefying α-amylases from Bacillus amyloliquefaciens (BAA), Bacillus licheniformis (BLA), and Bacillus stearothermophilus (BSTA), but has little homology to bacterial saccharifying α-amylases. The backbone structure of glucan 1,4-alpha-maltohexaosidase resembles the structure of bacterial liquefying α-amylases BLA and BSTA.

Glucan 1,4-alpha-maltohexaosidase plays a pivotal role in the production of G6 with low sweetness, low viscosity, and high efficiency for the uptake of energy by humans. This enzyme also can be used in the production of high maltose syrup. Moreover, glucan 1,4-alpha-maltohexaosidase has a potential application in detergent industry and serves as an important catalyst in the industrial production of p-nitrophenyl α-maltoheptaoside, which is a useful substrate for assay of human α-amylase in serum and urine. The enzyme has been widely studied for various applications, to which monitoring the enzyme activity is of fundamental importance.

Creative Enzymes has brought the accurate enzymatic activity measurement for glucan 1,4-alpha-maltohexaosidase. Our spectrophotometric assay is considered to be one of the most reliable methods for activity quantification, which is performed using the most advanced instrument. The unique and superior service distinguishes Creative Enzymes from our competitors. In the future, Creative Enzymes will continue supporting your business, helping to proceed toward achievements and success.

Figure: The crystal structure of glucan 1,4-alpha-maltohexaosidase from alkalophilic Bacillus sp.707.
PDB: 1WP6