Novel activity of Streptomyces aminopeptidase P
Abstract Streptomyces aminopeptidase P enzymes are proline-specific peptidases that belong to the peptidase M24 family. To evaluate the activity of a commercial Streptomyces aminopeptidase P, named ‘XPO DUET’, we performed three experiments involving degradation of tryptic casein, production of free...
Main Authors: | , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
SpringerOpen
2020-04-01
|
Series: | Bioresources and Bioprocessing |
Subjects: | |
Online Access: | http://link.springer.com/article/10.1186/s40643-020-00309-7 |
id |
doaj-6771e284911c460d8247a6480c5fa8c8 |
---|---|
record_format |
Article |
spelling |
doaj-6771e284911c460d8247a6480c5fa8c82020-11-25T02:39:04ZengSpringerOpenBioresources and Bioprocessing2197-43652020-04-01711810.1186/s40643-020-00309-7Novel activity of Streptomyces aminopeptidase PKun Wan0Misugi Uraji1Lingli Yang2Ryota Nakahigashi3Tadashi Hatanaka4Okayama Prefectural Technology Center for Agriculture, Forestry, and Fisheries, Research Institute for Biological Sciences (RIBS)Okayama Prefectural Technology Center for Agriculture, Forestry, and Fisheries, Research Institute for Biological Sciences (RIBS)Okayama Prefectural Technology Center for Agriculture, Forestry, and Fisheries, Research Institute for Biological Sciences (RIBS)Faculty of Agriculture, Nagase ChemteX CorporationOkayama Prefectural Technology Center for Agriculture, Forestry, and Fisheries, Research Institute for Biological Sciences (RIBS)Abstract Streptomyces aminopeptidase P enzymes are proline-specific peptidases that belong to the peptidase M24 family. To evaluate the activity of a commercial Streptomyces aminopeptidase P, named ‘XPO DUET’, we performed three experiments involving degradation of tryptic casein, production of free amino acids from casein hydrolysate, and hydrolysis of synthetic peptides. Using an ion-trap liquid chromatography–mass spectrometry (LC–MS) apparatus, we demonstrate that XPO DUET could degrade FFVAPFPEVFGK, an allergic and bitter peptide, VAPFPEVFGK, and PEVFGK from tryptic casein. All amino acids, except Ala, Asp, Glu, and Tyr, were released in an XPO DUET activity-dependent manner during the hydrolysis of casein hydrolysate. LC–MS analysis also revealed the ability of XPO DUET to completely hydrolyze Phe-Phe-Phe into free Phe. Thus, we confirm that XPO DUET possesses broader specificity than its known activity toward Xaa-Pro peptides. Because XPO DUET is a food-grade peptidase, it is useful in the bioprocessing of protein hydrolysates through its combination with other food-grade peptidases.http://link.springer.com/article/10.1186/s40643-020-00309-7Aminopeptidase PStreptomycesM24 family |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Kun Wan Misugi Uraji Lingli Yang Ryota Nakahigashi Tadashi Hatanaka |
spellingShingle |
Kun Wan Misugi Uraji Lingli Yang Ryota Nakahigashi Tadashi Hatanaka Novel activity of Streptomyces aminopeptidase P Bioresources and Bioprocessing Aminopeptidase P Streptomyces M24 family |
author_facet |
Kun Wan Misugi Uraji Lingli Yang Ryota Nakahigashi Tadashi Hatanaka |
author_sort |
Kun Wan |
title |
Novel activity of Streptomyces aminopeptidase P |
title_short |
Novel activity of Streptomyces aminopeptidase P |
title_full |
Novel activity of Streptomyces aminopeptidase P |
title_fullStr |
Novel activity of Streptomyces aminopeptidase P |
title_full_unstemmed |
Novel activity of Streptomyces aminopeptidase P |
title_sort |
novel activity of streptomyces aminopeptidase p |
publisher |
SpringerOpen |
series |
Bioresources and Bioprocessing |
issn |
2197-4365 |
publishDate |
2020-04-01 |
description |
Abstract Streptomyces aminopeptidase P enzymes are proline-specific peptidases that belong to the peptidase M24 family. To evaluate the activity of a commercial Streptomyces aminopeptidase P, named ‘XPO DUET’, we performed three experiments involving degradation of tryptic casein, production of free amino acids from casein hydrolysate, and hydrolysis of synthetic peptides. Using an ion-trap liquid chromatography–mass spectrometry (LC–MS) apparatus, we demonstrate that XPO DUET could degrade FFVAPFPEVFGK, an allergic and bitter peptide, VAPFPEVFGK, and PEVFGK from tryptic casein. All amino acids, except Ala, Asp, Glu, and Tyr, were released in an XPO DUET activity-dependent manner during the hydrolysis of casein hydrolysate. LC–MS analysis also revealed the ability of XPO DUET to completely hydrolyze Phe-Phe-Phe into free Phe. Thus, we confirm that XPO DUET possesses broader specificity than its known activity toward Xaa-Pro peptides. Because XPO DUET is a food-grade peptidase, it is useful in the bioprocessing of protein hydrolysates through its combination with other food-grade peptidases. |
topic |
Aminopeptidase P Streptomyces M24 family |
url |
http://link.springer.com/article/10.1186/s40643-020-00309-7 |
work_keys_str_mv |
AT kunwan novelactivityofstreptomycesaminopeptidasep AT misugiuraji novelactivityofstreptomycesaminopeptidasep AT lingliyang novelactivityofstreptomycesaminopeptidasep AT ryotanakahigashi novelactivityofstreptomycesaminopeptidasep AT tadashihatanaka novelactivityofstreptomycesaminopeptidasep |
_version_ |
1724787750970851328 |