SharePurification of tributyrin esterase from Lactococcus lactis subsp. cremoris E8.
Author(s) : HOLLAND R., COOLBEAR T.
Type of article: Article
Summary
The enzyme was purified by chromotography. Tributyrin esterase is active against tributyrin and butyrate of p-nitrophenyl. The N-terminal sequence of the enzyme was determined. The esterase has an optimal activity at neutral pH, is stable during freezing at -20 deg C and has a half-life of 1 hour at 50 deg C.
Details
- Original title: Purification of tributyrin esterase from Lactococcus lactis subsp. cremoris E8.
- Record ID : 1997-1696
- Languages: English
- Source: Asian J. Dairy Res. - vol. 63 - n. 1
- Publication date: 1996
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Indexing
- Themes: Milk and dairy products
- Keywords: Microbiology; Temperature; Purification; Dairy product; Ph; Enzyme
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