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Purification and characterization of diacetyl reductase from Kluyveromyces marxianus

✍ Scribed by J.G. Schwarz; Y.D. Hang

Book ID
115272248
Publisher
John Wiley and Sons
Year
1994
Tongue
English
Weight
374 KB
Volume
18
Category
Article
ISSN
0266-8254

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✍ J.G. Schwarz; Y.D. Hang 📂 Article 📅 1994 🏛 Springer 🌐 English ⚖ 235 KB

Kluyoeromyces mamianus had a higher specific activity of diacetyl reductase (EC 1.1.1.5) than all other organisms previously reported. The enzyme was NADH-dependent and irreversibly catalysed the conversion of diacetyl to acetoin with an optimum pH of 7.0. It was stable at 40°C but lost 50% of its a