Purification and characterization of a novel thermostable beta-amylase from Clostridium thermosulphurogenes.

An extracellular beta-amylase from Clostridium thermosulphurogenes was purified 811-fold to homogeneity, and its general molecular, physico-chemical and catalytic properties were determined. The native enzyme was a tetramer of 210 kDa composed of a single type subunit; its 20 amino acid N-terminus d...

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Detaylı Bibliyografya
Asıl Yazarlar: Shen, G J, Saha, B C, Lee, Y E, Bhatnagar, L, Zeikus, J G
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: 1988
Konular:
Research Article
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC1135158/
https://ncbi.nlm.nih.gov/pubmed/2461701
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