Enhancement of apparent thermostability of lipase from Rhizopus sp. by the treatment with a microbial transglutaminase

Noriho Kamiya, Takashi Ogawa, Teruyuki Nagamune

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Crude lipase from Rhizopus sp. was moderately stable against heat treatment at 45 °C. However, after incubation for 1 h at 25 °C with Streptoverticillium transglutaminase (MTG), the half-life of crude lipase in the heat treatment was increased more than 10-fold compared to that of untreated one. The result can be ascribed by the MTGasemediated crosslinking of contaminating proteins that affect the apparent thermostability of lipase in the crude sample.

Original languageEnglish
Pages (from-to)1629-1632
Number of pages4
JournalBiotechnology Letters
Volume23
Issue number19
DOIs
Publication statusPublished - 2001
Externally publishedYes

Fingerprint

Rhizopus
Transglutaminases
Lipases
Lipase
Hot Temperature
Heat treatment
Crosslinking
Half-Life
Proteins

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Applied Microbiology and Biotechnology
  • Microbiology
  • Bioengineering

Cite this

Enhancement of apparent thermostability of lipase from Rhizopus sp. by the treatment with a microbial transglutaminase. / Kamiya, Noriho; Ogawa, Takashi; Nagamune, Teruyuki.

In: Biotechnology Letters, Vol. 23, No. 19, 2001, p. 1629-1632.

Research output: Contribution to journalArticle

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