Characterization of cold- and high-pressure-active polygalacturonases from a deep-sea yeast, Cryptococcus liquefaciens strain N6

被引:24
作者
Abe, F
Minegishi, H
Miura, T
Nagahama, T
Usami, R
Horikoshi, K
机构
[1] JAMSTEC, Extremobiosphere Res Ctr, Yokosuka, Kanagawa 2370061, Japan
[2] Toyo Univ, Fac Engn, Dept Appl Chem, Kawagoe, Saitama 3500815, Japan
关键词
deep-sea yeast; Cryptococcus liquefaciens strain N6; polygalacturonase; high hydrostatic pressure;
D O I
10.1271/bbb.70.296
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A deep-sea yeast, Cryptococcus liquefaciens strain N6, produces two polygalacturonases, p36 and p40 (N6-PGases). These N6-PGases were highly active at 0-10 degrees C in comparison to a PGase from Aspergillus japonicus. The hydrolytic activity of these N6-PGases remained almost unchanged up to a hydrostatic pressure of 100 MPa at 24 degrees C with a very small activation volume of -1.1ml/mol. At 10 degrees C, however, the activation volume increased to 3.3 or 5.4ml/mol (p36 and p40, respectively), suggesting that the enzyme-substrate complexes can expand at their transition states. We speculate that such a volume expansion upon forming the enzyme-substrate complexes contributes to decreasing the activation energy for hydrolysis. This can account for the high activity of N6-PGases at low-temperature.
引用
收藏
页码:296 / 299
页数:4
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