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The N-terminally truncated GtfB enzyme of Lactobacillus fermentum NCC 2970 is a member of the GH70 family. The 4,3-α-glucanotransferase converts amylose and malto-oligosaccharides in an alternating glucan containing 60 % α(1→4) and 40 % α(1→3) glucosidic linkages, and α(1→3,4) branching points.
This product is sold for research use only.
*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.
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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.
This product is sold for research use only.
*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.
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The GtfD enzyme of the gram-negative bacteria Azotobacter chroococcum is a unique evolutionary intermediate between glycoside hydrolase family GH13 (α-amylase) and GH70 (glucansucrase). The enzyme displays 4,6-α-glucanotransferase activity using malto-oligosaccharides (> DP 4), and starch. However, the enzyme is unable to synthesize consecutive α(1→6) glucosidic bonds. Instead it forms a high molecular mass α(1→4,6) branched reuteran like polymer with 68 % α(1→4), and 32 % α(1→6) glycosidic linkages using amylose V as substrate. The glucan is highly similar to the product formed by Lactobacillus reuteri GtfA glucansucrase from sucrose. The products formed by the GtfD enzyme is potentially useful for the conversion of starch in the food industry.
This product is sold for research use only.
*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.
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The GtfC enzyme of Exiguobacterium sibiricum 255-15 is a member of the GH70 family. This glucanotransferase is active on malto-oligosaccharides and starch, synthesizing isomalto/malto-oligosaccharides (IMMOs) containing 52 % α(1→6) and 35 % α(1→4)-glycosidic linkages using amylose V. Biochemically, GtfC enzymes are close related to the GH70 GtfB enzymes. Although its domain organization is more closely related to GH13 enzymes (α-amylases). Making the GtfC 4,6-glucanotransferase an interesting intermediate between α-amylase and glucansucrase enzymes.
This product is sold for research use only.
*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.
