An unusual feruloyl esterase belonging to family VIII esterases and displaying a broad substrate range

Content Provider	Semantic Scholar
Author	Ohlhoff, Colin W. Casanueva, Ana Bauer, Rolene Cowan, Don Arthur Tuffin, Marla
Copyright Year	2014
Abstract	A thermophilic compost metagenomic library constructed in E. coli was functionally screened for novel esterases. Of the 110,592 fosmid clones screened, 25 clones demonstrated degradative activity on glyceryl tributyrate (a hit rate of 1:4,423). Four clones displayed ferulic acid esterase activity and were sequenced using 454 Titanium sequencing technology. EstG34, a 410 amino acid protein, was identified as having high sequence identity with a
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Alternate Webpage(s)	https://repository.up.ac.za/bitstream/handle/2263/48930/Ohlhoff_Unusual_2015.pdf;sequence=1
Language	English
Access Restriction	Open
Subject Keyword	Acetylesterase Amino Acids Biopolymer Sequencing Dot-com company Esterases Metagenomics Projection screen Sequence alignment Thrombocytopenia Titanium ferulic acid feruloyl esterase activity tributyrin
Content Type	Text
Resource Type	Article