~ 15 U/mg (40oC, pH 4.5 on potato galactan);~ 30 U/mg (60oC, pH 4.5 on potato galactan)One Unitof galactanase activity is defined as the amount of enzyme required to release one µmole of galactose reducing-sugar equivalents per minute from potato galactan in sodium acetate buffer (100 mM), pH 4.5.Applications established in diagnostics and research within the food and feed, carbohydrate and biofuels industries.High purity recombinantendo-1,4-β-Galactanase(Clostridium thermocellum)for use in research, biochemical enzyme assays andin vitrodiagnostic analysis.See all Carbohydrate Active enZYmes.Structural modifications of sugar beet pectin and the relationship of structure to functionality.Funami, T., Nakauma, M., Ishihara, S., Tanaka, R., Inoue, T. Phillips, G. O. (2011). Food Hydrocolloids, 25(2), 221-229.The emulsifying properties of sugar beet pectin (SBP) were investigated in relation to its molecular structure. SBP has been subjected to an enhancement process, and this material was here compared with conventional non-enhanced SBP. The oil-in-water emulsification properties of both were compared at 1.5% concentration at pH 3.25, using 15% middle-chain triglyceride as the oil phase. Their emulsification behavior after various enzyme treatments decreased in the order: protease arabinanase/galactanase mixture polygalacturonase. The enzyme treatment also decreased the molecular weight of SBP. Protease degraded the high molecular weight carbohydrate–protein complex. Arabinanase/galactanase mixture was more effective in decreasing the emulsification performance than polygalacturonase. The results confirm the key role of protein as the anchor for the oil droplets and identify also the contribution of the neutral lateral chains in stabilizing emulsions by forming a hydrated layer. Protein also aggregates, which functions as a linker for the association of the carbohydrate chains consequent to the enhancement process.Hide AbstractWe use cookies to give you the best possible experience on our site. By continuing to use the site you agree to our use of cookies.Moreinformation

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