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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Autori principali: 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
Natura: Artigo
Lingua:Inglês
Pubblicazione: American Society for Microbiology 2003
Soggetti:
Physiology and Biotechnology
Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC143600/
https://ncbi.nlm.nih.gov/pubmed/12571020
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/AEM.69.2.980-986.2003
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