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Purification and properties of three types of xylanases produced by an alkalophilic actinomycete
Author(s) -
Tsujibo H.,
Sakamoto T.,
Nishino N.,
Hasegawa T.,
Inamori Y.
Publication year - 1990
Publication title -
journal of applied bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 0021-8847
DOI - 10.1111/j.1365-2672.1990.tb01530.x
Subject(s) - isoelectric point , chemistry , chromatography , molecular mass , enzyme , polyacrylamide gel electrophoresis , sephadex , sodium , acetone , isoelectric focusing , xylan , electrophoresis , nuclear chemistry , biochemistry , organic chemistry
Three types of xylanases (l,4‐β‐D‐xylan xylanohydrolase, EC 3.2.1.8) were isolated from the culture filtrate of an alkalophilic actinornycete, Nocardiopsis dassonvillei subsp. alba OPC‐18. The enzymes (X‐I, X‐II and X‐III) were purified by acetone precipitation, chromatographies of DEAE‐cellulofine A‐800, Sephadex G‐75 and preparative isoelectric focusing. The purified enzymes showed single bands on sodium dodecyl sulphate polyacrylamide gel electrophoresis. The molecular weights of X‐I, X‐II and X‐III were 23000, 23000 and 37000, respectively. The pIs were 4.9 (X‐I), 5.3 (X‐II) and 4.1 (X‐III). The optimum pH levels for the activity of X‐I and X‐II were pH 7.0. X‐III was also most active at pH 7.0, but 62.5% of the activity remained even at pH 11. The optimum temperatures for the activities of X‐I and X‐II were 60°C and that of X‐III was 50°C. X‐I and X‐II were stable in the range of pH 6–10, and X‐III was stable in the range of pH 8–12 until 40°C for 30 min.