The GtfD 4,6-α-glucanotransferase enzyme of Paenibacillus beijingensis is a member of the glycoside hydrolase family 70. It produces two reuteran-like polymers distributions that were generated from amylose V: a high-molecular-mass polymer (HMMP) and a low-molecular mass polymer (LMMP) containing both long linear α(1→4) chains. The HMM polymer with an average length of 27 MDa contains 71 % α(1→4) and 29 % α(1→6)linkages. While the LMM polymer of 19 KDa consists of 77 % α(1→4) and 23 % α(1→6) linkages. Indicating the HMM has a slightly higher amount of α(1→6) linkages.

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*Enzyme activity was determined by the iodine-staining assay using amylose as substrate. One unit of activity is defined as the amount of enzyme preparation converting 1 mg of substrate per min.