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J. Biochem, 1977, Vol. 81, No. 3 539-546
© 1977 Japanese Biochemical Society

research-article

Multiple Components of Endo-polyguluronide Lyase of Pseudomonas sp.

Kyung Hee MIN1, Sonoko F. SASAKI2, Yoshiko KASHIWABARA3, Hiroshi SUZUKI and Kazutosi NISIZAWA4

Department of Botany, Faculty of Science, Tokyo Kyoiku University Otsuka, Bunkyo-ku, Tokyo 112

A lyophilized alginate lyase preparation obtained from dialyzed extract of sonicated Pseudomonas sp. cells was fractionated by gel filtration on a Sephadex G-150 column, and three alginate lyase [EC 4.2.2.3 [EC] ] fractions, peaks I, II, and III, were obtained. They were remarkably thermolabile. The lyase fractions degraded two kinds of alginate fragments, a polyguluronide (SG), and a polyuronide consisting of both mannuronic and guluronic acid residues (SMG), as well as commercial alginate, but were virtually inactive toward polymannuronide fragment (SM). The modes of degradation of these substrates by the lyase fractions were endowise with different degrees of randomness. Attack by the peak I fraction was more random than those by peaks II and III. The main lysis products formed from SG and SMG by these layses were identified as mixtures of unsaturated tri- and monouronides. The unsaturated triuronide from SG was {delta}UGG and SMG yielded a mixture of {delta}UGG and a poorly characterized unsaturated trimer, possibly {delta}UMG. However, the patterns of monomer and trimer production by these lyase fractions changed in different ways during incubation.

1Present address: Department of Biology, College of Liberal Arts and Sciences, Suk-Mung Women's University, Seoul, Korea.

2Present address: Department of Home Science, Faculty of Humanity and Culture, Tokai University, Hiratsuka, Kanagawa 254.

3Present address: National Institute for Leprosy Research, Higashimurayama, Tokyo 189.

4Present address: Department of Fisheries, College of Agriculture and Veterinary Medicine, Nihon University, Setagaya-ku, Tokyo 154.


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