Laminarin enzymic hydrolysis

Barry114 isolated a disaccharide, laminaribiose, on the partial hydrolysis of laminarin by enzymes (digestive juice of the snail Helix pomatia or H. aspersa) or by acid (seven hours with N oxalic acid on the water-bath). He showed that this disaccharide consisted solely of D-glucose and considered it to be 3-j3-D-glucopyranosyl-D-glucopyranose (XXIX). 

Another purified enzyme preparation which produces laminaripentaose from insoluble laminarin and from heat-treated pachyman is produced by a strain of Arthrobacter luteus (100,101,102) when grown on yeast cells or / -(1 —>3)-glucan. The enzyme, which was named Zymolase (also referred to as Zymolyase) appeared to be homogeneous by electrophoresis in a Tiselius apparatus and by ultracentrifugation. The molecular weight of the enzyme was estimated from ultracentrifugation to be ca. 20,500. The optimum pH for lysis of viable yeast cells was 7.5. The optimum temperature was 35°C. The optimum pH for heat-treated pachyman hydrolysis was 6.5, and the optimum temperature was 45°C. A Lineweaver-Burk plot with heat-treated pachyman yielded a Km value of 0.04% when the solubilized carbohydrate was assayed by the phenol-sulfuric acid method. Zymolase lost all its activity after incubation at 60°C for 5 min. 

---