Abstract
SUMMARYA new type of endo‐pectic acid transeliminase was isolated from the culture medium of a strain of Bacillus. The enzyme attacked pectic substances randomly and produced un saturated trigalacturonic acid as the major end product. The optimum pH on either acid‐soluble pectic acid or tetragalaeturonic acid was 9.3–9.7, and the enzyme required calcium ions for maximum activity. Strontium was the only other divalent cation which stimulated activity. Trigalacturonic acid was attacked very slowly. The major site of attack of tetragalacturonic acid was the glycosidic bond on the nonreducing end. Unsaturated tetragalacturonic acid was also attacked at the central bond. The cleavage of pentagalacturouic acid occurred preferentially at bond 3, followed by 4 and 2, in order. The glycosidic bond on the reducing end is called bond 1. With unsaturated pentagalacturonic acid, it was concluded that the major site of cleavage was at bond 3, with a much slower rate at bond 2.
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