Hydrophobic interactions between the secondary structures on the molecular surface reinforce the alkaline stability of serine protease

Yuki Oguchi, Hiroshi Maeda, Keietsu Abe, Tasuku Nakajima, Takafumi Uchida, Youhei Yamagata

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

We employed random mutagenesis to determine the region of the initial unfolding of hyper-alkaline-sensitive subtilisin, ALP I, that precedes the denaturation of the entire protein under highly alkaline conditions. This region comprises two α-helices and a calcium-binding loop. Stabilization of the region caused the stabilization of the entire protein at a high alkaline pH 12. The alkaline stability of this region was most effectively improved by hydrophobic interactions, followed by ionic interactions with Arg residues. The effect of mutations on the improvement was different with regard to the alkaline stability and thermostability. This indicated that different strategies were necessary to improve the alkaline stability and thermostability of the protein.

Original languageEnglish
Pages (from-to)1383-1391
Number of pages9
JournalBiotechnology Letters
Volume28
Issue number17
DOIs
Publication statusPublished - 2006 Sep 1

Keywords

  • Alkaline stability
  • Hydrophobic interaction
  • Protein structure
  • Secondary structures
  • Subtilisin

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

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