Molecular weight distribution and fermentation of mechanically pre-treated konjac enzymatic hydrolysates.

There is interest in novel fibers as potential prebiotics for new and reformulated food products. Two konjac glucomannan (KGM) hydrolysates were developed by enzymatic hydrolysis with (KGMH I) or without (KGMH II) mechanical shear pre-treatment. These were characterized and evaluated as fermentation substrates using five lactobacilli and three bifidobacteria. Enzymatic treatment of native KGM reduced the average molecular weights of supernatant and pellet by ∼3-fold. Additional mechanical shear pre-treatment further reduced supernatant and pellet molecular weights by 5% and 35%, respectively. We postulated that pulverized and depolymerized short-chain KGM would better promote the growth of lactobacilli and bifidobacteria. Most lactobacilli fermented KGM hydrolysates. Lactobacillus acidophilus and Lactobacillus plantarum fermented KGMH I and II better than they fermented inulin. Overall, bifidobacteria were not strong fermenters of KGM hydrolysates. Both pulverization and enzymatic depolymerization significantly affected KGM molecular weight, suggesting that human gastrointestinal bacteria can utilize KGM hydrolysates with reduced weights.

Proteomic identification of a basic peroxidase stabilized within acetylated polymannan polysaccharide of Aloe barbadensis.

Acetylated polymannan polysaccharide (ApmP) isolated from Aloe barbadensis Miller contains a stable peroxidase that was solubilized to investigate its biochemical, electrophoretic, immunological, and proteomic properties. In the electrophoretic band corresponding to the solubilized peroxidase, proteomic analysis detected seven tryptic peptides that matched homologous peptides covering one third of the ATP22a peroxidase of Arabidopsis thaliana. All the characteristics tested indicated that the activity stabilized within the ApmP pertains to the basic secretory peroxidase family, which includes members that have several biotechnological uses. Hence ApmP might yield a widely used peroxidase in stabilized form.

Aleppo tannin: structural analysis and salivary amylase inhibition.

The effectiveness and specificity of a tannin inhibition on human salivary amylase (HSA) catalyzed hydrolysis was studied using 2-chloro-4-nitrophenyl 4-O-beta-D-galactopyranosyl-alpha-maltoside (GalG(2)-CNP) and amylose substrates. Aleppo tannin was isolated from the gall nut of Aleppo oak. This tannin is a gallotannin, in which glucose is esterified with gallic acids. This is the first kinetic report, which details the inhibitory effects of this compound on HSA. A mixed non-competitive type inhibition has been observed on both substrates. The extent of inhibition is markedly dependent on the substrate-type. Kinetic constants were calculated from Lineweaver-Burk secondary plots for GalG(2)-CNP (K(EI) 0.82 microg mL(-1), K(ESI) 3.3 microg mL(-1)). This indicates a 1:1 binding ratio of inhibitor-enzyme and/or inhibitor-enzyme-substrate complex. When amylose was the substrate the binding ratio of inhibitor to enzyme-substrate complex was found to be 2:1, with the binding constants of K(EI) 17.4 microg mL(-1), K(ESI) 14.9 microg mL(-1), K(ESI(2)) 9.6 microg mL(-1). Presumably, the tannin inhibitor can bind not only to HSA, but to the amylose substrate, as well. Kinetic data suggest that Aleppo tannin is a more efficient amylase inhibitor than the recently studied other tannin with quinic acid core (GalG(2)-CNP: K(EI) 9.0 microg mL(-1), K(ESI) 47.9 microg mL(-1)).