Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Biochemistry & Molecular Biology Regular Papers
Purification and Characterization of Novel Transglutaminase from Bacillus subtilis Spores
Shun'ichi SUZUKIYuko IZAWAKatusnori KOBAYASHIYuzuru ETOShigeru YAMANAKAKoji KUBOTAKenzo YOKOZEKI
Author information
JOURNAL FREE ACCESS

2000 Volume 64 Issue 11 Pages 2344-2351

Details
Abstract

  Transglutaminase activity was detected in suspensions of purified spores prepared from lysozyme-treated sporulating cells of Bacillus subtilis AJ 1307. The enzyme was easily solubilized from the spores upon incubation at pH 10.5 at 37°C. The transglutaminase activity was separated into two fractions upon purification by hydrophobic interaction chromatography (TG1 and TG2). Each enzyme was purified to electrophoretic homogeneity (about 1,000-fold). Both enzymes had the same molecular weight of 29,000 as estimated by SDS-PAGE, had the same N-terminal 30 amino acid sequence, and also showed the same optimal temperature (60°C) and pH (8.2). The purified enzyme catalyzed formation of cross-linked ε-(γ-glutamyl)lysine isopeptides, resulting in the gel-formation of protein solutions such as αs-casein and BSA.

Content from these authors

This article cannot obtain the latest cited-by information.

© 2000 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
Previous article Next article
feedback
Top