Characterization of a Thermostable d-Stereospecific Alanine Amidase from Brevibacillus borstelensis BCS-1

A gene encoding a new thermostable d-stereospecific alanine amidase from the thermophile Brevibacillus borstelensis BCS-1 was cloned and sequenced. The molecular mass of the purified enzyme was estimated to be 199 kDa after gel filtration chromatography and about 30 kDa on sodium dodecyl sulfate-pol...

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Publié dans:	Appl Environ Microbiol
Auteurs principaux:	Baek, Dae Heoun, Kwon, Seok-Joon, Hong, Seung-Pyo, Kwak, Mi-Sun, Lee, Mi-Hwa, Song, Jae Jun, Lee, Seung-Goo, Yoon, Ki-Hong, Sung, Moon-Hee
Format:	Artigo
Langue:	Inglês
Publié:	American Society for Microbiology (ASM) 2003
Sujets:	Physiology and Biotechnology
Accès en ligne:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC143600/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/12571020/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/AEM.69.2.980-986.2003
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