O-D-mannopyranosyl-(1→4)-O-D-glucopyranosyl-(1→4)-D-Mannopyranose (MGM) was prepared via the enzymatic hydrolysis of konjac glucomannan and the subsequent elimination of monosaccharides from the resultant hydrolysate using yeast. The enzyme system hydrolyzed konjac glucomannan and produced monosaccharides and MGM without other oligomers at the 48 h reaction. Konjac 20 g was hydrolyzed at 60 o C and a pH 6.0 for 48 h with 200 mL crude enzyme solution from Xylogone sphaerospora. By eliminating monosaccharides from the hydrolysis products with yeast (Candida guilliermondii), 3.8 g of crystalline MGM was obtained, without the use of chromatographic techniques. After 48 h of yeast cultivation, the total sugar content fell from 5.2% to 3.7%, while the average degree of polymerization (D.P.) rose from 2.6 to 3.3.

xylanolytic gut bacterium isolated from Eisenia fetida, Cellulosimicrobium sp. strain HY-13, produced an extracellular glycoside hydrolase capable of efficiently degrading mannose-based substrates such as locust bean gum (LBG), guar gum, mannotetraose, and mannopentaose. The purified mannan-degrading enzyme (ManS, 34,926 Da) from strain HY-13 was found to have an N-terminal amino acid sequence of DEATTDGLHVVDD, which has not yet been identified. Under the optimized reaction conditions of 50℃ and pH 7.0, ManK exhibited extraordinary high specific activities of 7,109 IU/mg and 5,158 IU/mg toward LBG and guar gum, respectively, while the enzyme showed no effect on sugars substituted with p-nitrophenol and various non-mannose carbohydrates. ManK strongly attached to Avicel, lignin, β-cyclodextrin, and poly(3-hydroxybutyrate) granules, but not bound to chitin, chitosan, curdlan, or insoluble oat spelt xylan. The aforementioned characteristics of ManS suggest that it is a unique endo-β -1,4-mannanase with out additional carbohydrolase activities, which differentiates it from other well-known carbohydrolases.