Ability of T1 lipase to degrade amorphous P(3HB): structural and functional study
An enzyme with broad substrate specificity would be an asset for industrial application. T1 lipase apparently has the same active site residues as polyhydroxyalkanoates (PHA) depolymerase. Sequences of both enzymes were studied and compared, and a conserved lipase box pentapeptide region around the...
Saved in:
Main Authors: | A. Mohamed, Rauda, Salleh, Abu Bakar, Thean, Adam Chor Leow, Mohd Yahaya, Normi, Abdul Rahman, Mohd Basyaruddin |
---|---|
Format: | Article |
Language: | English |
Published: |
Humana Press
2017
|
Online Access: | http://psasir.upm.edu.my/id/eprint/60757/1/Ability%20of%20T1%20lipase%20to%20degrade%20amorphous%20P%283HB%29%20structural%20and%20functional%20study.pdf http://psasir.upm.edu.my/id/eprint/60757/ https://link.springer.com/content/pdf/10.1007%2Fs12033-017-0012-0.pdf |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Recent advances in overexpression of functional recombinant lipases
by: Alias, Fatin Liyana, et al.
Published: (2023) -
Engineering lipase for structure and function relationship study
by: Ahmad Kamarudin, Nor Hafizah, et al.
Published: (2017) -
Thermostable lipases and their dynamics of improved enzymatic properties
by: Hamdan, Siti Hajar, et al.
Published: (2021) -
Thermostable lipases
by: Leow, Adam Thean Chor, et al.
Published: (2006) -
Shifting the pH profiles of Staphylococcus epidermidis lipase (SEL) and Staphylococcus hyicus lipase (SHL) through generating chimeric lipases by DNA shuffling strategy
by: Wan Hasan, Wan Atiqah Najiah, et al.
Published: (2024)