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Substrate specifcity of alkaline protease from alkaliphilic feather-degrading Nesterenkonia sp AL20

Bakhtiar, Shahrzad LU ; Estiveira, RJ and Hatti-Kaul, Rajni LU (2005) In Enzyme and Microbial Technology 37(5). p.534-540
Abstract
The substrate specificity of an alkaline protease, produced by Nesterenkonia sp. AL20 grown on chicken feather as the nutrient source, was assessed using oxidized insulin B-chain and derivatized peptide substrates. The initial cleavage of the. insulin chain was determined to be at Tyr(16) -Leu(17) and Tyr(26) -Thr(27), followed by Gln(4)-His(5), Phe(25)-Tyr(26) and Leu(15)-Tyr(16) bonds. An additional cleavage site at Ser(9)-His(10) was found during hydrolysis for a long time. Among the peptide substrates, the enzyme exhibited activity mainly with tetrapeptide substrates with hydrophobic residues located at P1 site in the order Tyr > Phe > Len. Decreasing the size of the peptide resulted in a drastic reduction of activity, suggesting... (More)
The substrate specificity of an alkaline protease, produced by Nesterenkonia sp. AL20 grown on chicken feather as the nutrient source, was assessed using oxidized insulin B-chain and derivatized peptide substrates. The initial cleavage of the. insulin chain was determined to be at Tyr(16) -Leu(17) and Tyr(26) -Thr(27), followed by Gln(4)-His(5), Phe(25)-Tyr(26) and Leu(15)-Tyr(16) bonds. An additional cleavage site at Ser(9)-His(10) was found during hydrolysis for a long time. Among the peptide substrates, the enzyme exhibited activity mainly with tetrapeptide substrates with hydrophobic residues located at P1 site in the order Tyr > Phe > Len. Decreasing the size of the peptide resulted in a drastic reduction of activity, suggesting the enzyme to possess relatively narrow substrate specificity in comparison to several other serine proteases. AL20 protease showed good activity towards casein and hemoglobin as substrates, low activity with keratin azure, and poor activity with elastin-orcein. (c) 2005 Elsevier Inc. All rights reserved. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Enzyme and Microbial Technology
volume
37
issue
5
pages
534 - 540
publisher
Elsevier
external identifiers
  • wos:000231557800010
  • scopus:23744469373
ISSN
0141-0229
DOI
10.1016/j.enzmictec.2005.04.003
language
English
LU publication?
yes
id
cde5b2b9-abce-4d05-bb90-c3b927a14863 (old id 155064)
date added to LUP
2007-06-29 15:52:13
date last changed
2017-01-01 04:52:57
@article{cde5b2b9-abce-4d05-bb90-c3b927a14863,
  abstract     = {The substrate specificity of an alkaline protease, produced by Nesterenkonia sp. AL20 grown on chicken feather as the nutrient source, was assessed using oxidized insulin B-chain and derivatized peptide substrates. The initial cleavage of the. insulin chain was determined to be at Tyr(16) -Leu(17) and Tyr(26) -Thr(27), followed by Gln(4)-His(5), Phe(25)-Tyr(26) and Leu(15)-Tyr(16) bonds. An additional cleavage site at Ser(9)-His(10) was found during hydrolysis for a long time. Among the peptide substrates, the enzyme exhibited activity mainly with tetrapeptide substrates with hydrophobic residues located at P1 site in the order Tyr > Phe > Len. Decreasing the size of the peptide resulted in a drastic reduction of activity, suggesting the enzyme to possess relatively narrow substrate specificity in comparison to several other serine proteases. AL20 protease showed good activity towards casein and hemoglobin as substrates, low activity with keratin azure, and poor activity with elastin-orcein. (c) 2005 Elsevier Inc. All rights reserved.},
  author       = {Bakhtiar, Shahrzad and Estiveira, RJ and Hatti-Kaul, Rajni},
  issn         = {0141-0229},
  language     = {eng},
  number       = {5},
  pages        = {534--540},
  publisher    = {Elsevier},
  series       = {Enzyme and Microbial Technology},
  title        = {Substrate specifcity of alkaline protease from alkaliphilic feather-degrading Nesterenkonia sp AL20},
  url          = {http://dx.doi.org/10.1016/j.enzmictec.2005.04.003},
  volume       = {37},
  year         = {2005},
}