Thermally induced disintegration of the bacillus stearothermophilus dihydrolipoamide dehydrogenase

Yasuaki Hiromasa, Yoichi Aso, Shoji Yamashita, Kohji Meno

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Upon heat treatment of the pyruvate dehydrogenase complex from Bacillus stearothermophilus, the most thermostable component is a dihydrolipoamide dehydrogenase (E3c). To understand this stability, the thermal disintegration of E3 dissociated from the complex (E3d) was examined, comparing with that of E3c. Judging from residual activity and inactivation rate, E3d was less thermostable than E3c; E3d and E3c lost half of their original activities upon incubations for 30 min at 79°C and 90°C, respectively. Heat treatment of E3d raised the fluorescence intensities of Trp residue, intrinsic FAD, and extrinsic 8-anilinonaphthalene-1-sulfonate. E3d lost FAD, and inactive E3d polypeptides were aggregated. The sulfonate bound to the aggregate became notably fluorescent. The thermal disintegration of E3d was speculated to be a consecutive reaction that was different from the concurrent disintegration reaction of the complex. Some interactions with other component polypeptides was suggested to improve the thermostability of E3c.

Original languageEnglish
Pages (from-to)1923-1929
Number of pages7
JournalBioscience, Biotechnology and Biochemistry
Volume64
Issue number9
DOIs
Publication statusPublished - Jan 1 2000

Fingerprint

Dihydrolipoamide Dehydrogenase
Geobacillus stearothermophilus
Disintegration
Bacilli
Flavin-Adenine Dinucleotide
Hot Temperature
Heat treatment
Pyruvate Dehydrogenase Complex
Peptides
Fluorescence

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

Cite this

Thermally induced disintegration of the bacillus stearothermophilus dihydrolipoamide dehydrogenase. / Hiromasa, Yasuaki; Aso, Yoichi; Yamashita, Shoji; Meno, Kohji.

In: Bioscience, Biotechnology and Biochemistry, Vol. 64, No. 9, 01.01.2000, p. 1923-1929.

Research output: Contribution to journalArticle

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AB - Upon heat treatment of the pyruvate dehydrogenase complex from Bacillus stearothermophilus, the most thermostable component is a dihydrolipoamide dehydrogenase (E3c). To understand this stability, the thermal disintegration of E3 dissociated from the complex (E3d) was examined, comparing with that of E3c. Judging from residual activity and inactivation rate, E3d was less thermostable than E3c; E3d and E3c lost half of their original activities upon incubations for 30 min at 79°C and 90°C, respectively. Heat treatment of E3d raised the fluorescence intensities of Trp residue, intrinsic FAD, and extrinsic 8-anilinonaphthalene-1-sulfonate. E3d lost FAD, and inactive E3d polypeptides were aggregated. The sulfonate bound to the aggregate became notably fluorescent. The thermal disintegration of E3d was speculated to be a consecutive reaction that was different from the concurrent disintegration reaction of the complex. Some interactions with other component polypeptides was suggested to improve the thermostability of E3c.

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