Partial purification and some properties of a cellulase from Helix pomatia.

The properties of cellulases from Helix pomatia have been studied by many workers, including Seilliere (1906), Karrer, Schubert & Wehrli (1925), Karrer & Schubert (1926, 1928) and de Stevens (1955). Cellulolytic enzymes have also been found in other invertebrates, such as Teredo (Greenfield, 1955) and Ctenolep8ima lineata (Lasker & Giese, 1956), and in a wide range ofmicro-organisms which include some rumen Protozoa (Hungate, 1942) and bacteria (Halliwell, 1957 a, b). Many fungi, for example A8pergillus oryzae (Gillespie & Woods, 1953) andMyrothecium verrucaria (Saunders, Siu & Genest, 1948; Whitaker, 1953; Miller & Blum, 1956; Grimes, Duncan & Hoppert, 1957), have also been shown to produce cellulases. Although twofold purifications of H. pomatia (de Stevens, 1955) and Teredo (Greenfield, 1955) cellulases have been reported, only the cellulase from M. verrucaria has been purified to give an electrophoretically homogeneous protein (Whitaker, 1953). The properties of this enzyme have been extensively studied; its molecular weight is 63 000 + 15 000 (Whitaker, 1952; Basu & Whitaker, 1953; Whitaker, Colvin & Cook, 1954). The enzyme attacks many P-1:4-linked glucosans in an essentially random manner (Whitaker, 1954a, b, 1956 a, b, 1957; Whitaker & Merler, 1956), although there are deviations from this mode of attack with soluble oligosaccharides. The purified enzyme also attacks wheat-straw xylan (Adams, 1952). The present work was undertaken to purify cellulase from H. pomatia, often a more readily available source than a fungal-culture filtrate, and to compare its properties with those of the enzyme from M. verrucaria.