Purification and Characterization of Thermostable Pectate Lyase with Protopectinase Activity from Thermophilic Bacillus sp. TS 47 | Zendy

Makoto Takao | Zendy; Tetsuko Nakaniwa | Zendy; Kentaro Yoshikawa | Zendy; Takao Terashita | Zendy; Takuo Sakai | Zendy

Open Access

Purification and Characterization of Thermostable Pectate Lyase with Protopectinase Activity from Thermophilic Bacillus sp. TS 47

Author(s) -

Makoto Takao,

Tetsuko Nakaniwa,

Kentaro Yoshikawa,

Takao Terashita,

Takuo Sakai

Publication year - 2000

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.64.2360

Subject(s) - isoelectric point , bacillus subtilis , pectate lyase , thermophile , molecular mass , enzyme , chemistry , enzyme assay , strain (injury) , biochemistry , bacteria , chromatography , bacillales , biology , pectinase , anatomy , genetics

A strain of thermophilic bacterium, Bacillus sp., with pectolytic activity has been isolated. It produced an extracellular endo-polygalacturonate trans-eliminase (PL, EC 4.2.2.1) when grown at 60 degrees C on a medium containing polygalacturonate (PGA). The PL was purified by hydrophobic, cation exchange, and size exclusion column chromatographies. The molecular mass of the enzyme was 50 kDa by SDS-PAGE. The isoelectric point of the enzyme was pH 5.3. The enzyme had a half-life of 13 and 1 h at 65 and 70 degrees C, respectively, and showed optimal activity around at 70 degrees C and pH 8.0. It had protopectinase activity, besides PL activity, on lemon protopectin and cotton fibers. The first 20 amino acids sequence of the enzyme had significant similarity with that of PL from methophilic Bacillus subtilis, with 50% identity.

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