Abstract
Two novel endo-type polygalacturonases (PGase), with molecular weights of 36 kDa and 40 kDa (named p36 and p40, respectively), were purified from the supernatant of the culture medium of a deep-sea yeast, strain N6, isolated from the Japan Trench. The N-terminal 20 amino acids of p36 and p40 were identical, and the sequence homology was 47.4% in comparison with the PGase of Fusarium moniliforme. A treatment of p40 with glycopeptidase F reduced the molecular weight to 36 kDa, suggesting that p40 possessed N-acetylglucosamines on its asparagine residues and p40 might be matured by glycosylation of p36.
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Miura, T., Abe, F., Inoue, A. et al. Purification and characterization of novel extracellular endopolygalacturonases from a deep-sea yeast, Cryptococcus sp. N6, isolated from the Japan Trench. Biotechnology Letters 23, 1735–1739 (2001). https://doi.org/10.1023/A:1012488115482
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DOI: https://doi.org/10.1023/A:1012488115482