NDLI: Functional analysis of a hybrid endoglucanase of bacterial origin having a cellulose binding domain from a fungal exoglucanase

Content Provider	Springer Nature Link
Author	Kim, Hoon Goto, Masatoshi Jeong, Heo Jin Jung, Kyung Hwa Furukawa, Kensuke
Copyright Year	1999
Abstract	A cellulose binding domain (CBD) of an endo-β-l,4-glucanase (Ben) from the bacteriumBacillus subtilis BSE616 was replaced with the CBD of exoglucanase I (TexI) from the fungusTrichoderma viride HK-75. The resultant hybrid enzyme Ben’-CBD$_{TexI}$, comprising the catalytic domain (Ben’) of Ben and the CBD (CBD$_{TexI}$) of TexI, was highly expressed at 20% of the total protein inEscherichia coli. The molecular mass of the hybrid enzyme was estimated to be ca. 38 kDa by SDS-PAGE, which was in good agreement with that calculated from 305 amino acids of Ben and 42 amino acids of CBD$_{TexI}$. The hybrid enzyme exhibited almost the same activity as that of the original Ben toward soluble substrates, such as cellooligosaccharides. The hybrid enzyme showed higher binding ability and hydrolysis activity toward microcrystalline cellulose (Avicel), even though the length of the CBD of TexI was four times smaller than that of Ben. The hybrid enzyme was more resistant to tryptic digestion than the original Ben. The efficient binding ability of the hybrid enzyme to Avicel permitted purification of the enzyme using an Avicel-affinity column to the extent of ca. 90% purity.
Starting Page	193
Ending Page	204
Page Count	12
File Format	PDF
ISSN	02732289
Journal	Applied Biochemistry and Biotechnology
Volume Number	75
Issue Number	2-3
e-ISSN	15590291
Language	English
Publisher	Humana Press
Publisher Date	1999-01-01
Publisher Place	Totowa
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Biotechnology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Environmental Engineering Biochemistry Bioengineering Applied Microbiology and Biotechnology Biotechnology

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