Muskox myoglobin: purification, characterization and kinetics studies compared with cattle and water buffalo myoglobins
BACKGROUND The Arctic muskox has economic potential as an alternative meat species and is becoming increasingly popular. The present study aimed to determine the primary structure and pseudoperoxidase activity of muskox myoglobin (Mb) compared to cattle and water buffalo myoglobins. RESULTS The prim...
Published in: | Journal of the Science of Food and Agriculture |
---|---|
Main Authors: | , , , , , , , |
Other Authors: | , , , , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
2019
|
Subjects: | |
Online Access: | https://hdl.handle.net/11591/414489 https://doi.org/10.1002/jsfa.9901 http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1097-0010 |
id |
ftuncampaniairis:oai:iris.unicampania.it:11591/414489 |
---|---|
record_format |
openpolar |
spelling |
ftuncampaniairis:oai:iris.unicampania.it:11591/414489 2024-04-14T08:08:17+00:00 Muskox myoglobin: purification, characterization and kinetics studies compared with cattle and water buffalo myoglobins Ragucci S. Russo R. Landi N. Valletta M. Chambery A. Esposito S. Raundrup K. Di Maro A. Ragucci, S. Russo, R. Landi, N. Valletta, M. Chambery, A. Esposito, S. Raundrup, K. Di Maro, A. 2019 https://hdl.handle.net/11591/414489 https://doi.org/10.1002/jsfa.9901 http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1097-0010 eng eng info:eu-repo/semantics/altIdentifier/pmid/31259416 info:eu-repo/semantics/altIdentifier/wos/WOS:000480439100001 volume:99 issue:14 firstpage:6278 lastpage:6286 numberofpages:9 journal:JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE https://hdl.handle.net/11591/414489 doi:10.1002/jsfa.9901 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-85070715800 http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1097-0010 Bovidae MALDI-TOF MS myoglobin Ovibos moschatu info:eu-repo/semantics/article 2019 ftuncampaniairis https://doi.org/10.1002/jsfa.9901 2024-03-21T16:15:52Z BACKGROUND The Arctic muskox has economic potential as an alternative meat species and is becoming increasingly popular. The present study aimed to determine the primary structure and pseudoperoxidase activity of muskox myoglobin (Mb) compared to cattle and water buffalo myoglobins. RESULTS The primary structure of muskox Mb was determined via a matrix-assisted laser desorption ionization-time of flight mass spectrometry-based mapping approach using the sheep Mb as a reference sequence. The muskox Mb consists of 153 amino acid residues and shows 100% identity with sheep Mb, whereas 98.69% and 97.38% identity is found with cattle and water buffalo Mbs, respectively. Muskox Mb has an autoxidation rate (MetMb formation) higher than both cattle and water buffalo Mbs at pH 7.2 (37 degrees C). Moreover, its pseudoperoxidase activity is higher than both cattle and water buffalo Mbs at pH 7.4 (physiological pH), whereas it is slightly lower than cattle Mb and higher than water buffalo at a lower pH (5.8), corresponding to the conditions in meat. CONCLUSION For the first time, the present study reports the purification of myoglobin from muskoxen and, furthermore, a comparative study is conducted on autoxidation and pseudoperoxidase activity with respect to cattle and water buffalo Mbs at both physiological and acid pH. Overall, the results of the current research provide novel information for future studies useful to the meat industry when considering the importance of myoglobin as a principal pigment in meat colour stability. (c) 2019 Society of Chemical Industry Article in Journal/Newspaper Arctic muskox Università degli Studi della Campania "Luigi Vanvitelli": CINECA IRIS V: Arctic Journal of the Science of Food and Agriculture 99 14 6278 6286 |
institution |
Open Polar |
collection |
Università degli Studi della Campania "Luigi Vanvitelli": CINECA IRIS V: |
op_collection_id |
ftuncampaniairis |
language |
English |
topic |
Bovidae MALDI-TOF MS myoglobin Ovibos moschatu |
spellingShingle |
Bovidae MALDI-TOF MS myoglobin Ovibos moschatu Ragucci S. Russo R. Landi N. Valletta M. Chambery A. Esposito S. Raundrup K. Di Maro A. Muskox myoglobin: purification, characterization and kinetics studies compared with cattle and water buffalo myoglobins |
topic_facet |
Bovidae MALDI-TOF MS myoglobin Ovibos moschatu |
description |
BACKGROUND The Arctic muskox has economic potential as an alternative meat species and is becoming increasingly popular. The present study aimed to determine the primary structure and pseudoperoxidase activity of muskox myoglobin (Mb) compared to cattle and water buffalo myoglobins. RESULTS The primary structure of muskox Mb was determined via a matrix-assisted laser desorption ionization-time of flight mass spectrometry-based mapping approach using the sheep Mb as a reference sequence. The muskox Mb consists of 153 amino acid residues and shows 100% identity with sheep Mb, whereas 98.69% and 97.38% identity is found with cattle and water buffalo Mbs, respectively. Muskox Mb has an autoxidation rate (MetMb formation) higher than both cattle and water buffalo Mbs at pH 7.2 (37 degrees C). Moreover, its pseudoperoxidase activity is higher than both cattle and water buffalo Mbs at pH 7.4 (physiological pH), whereas it is slightly lower than cattle Mb and higher than water buffalo at a lower pH (5.8), corresponding to the conditions in meat. CONCLUSION For the first time, the present study reports the purification of myoglobin from muskoxen and, furthermore, a comparative study is conducted on autoxidation and pseudoperoxidase activity with respect to cattle and water buffalo Mbs at both physiological and acid pH. Overall, the results of the current research provide novel information for future studies useful to the meat industry when considering the importance of myoglobin as a principal pigment in meat colour stability. (c) 2019 Society of Chemical Industry |
author2 |
Ragucci, S. Russo, R. Landi, N. Valletta, M. Chambery, A. Esposito, S. Raundrup, K. Di Maro, A. |
format |
Article in Journal/Newspaper |
author |
Ragucci S. Russo R. Landi N. Valletta M. Chambery A. Esposito S. Raundrup K. Di Maro A. |
author_facet |
Ragucci S. Russo R. Landi N. Valletta M. Chambery A. Esposito S. Raundrup K. Di Maro A. |
author_sort |
Ragucci S. |
title |
Muskox myoglobin: purification, characterization and kinetics studies compared with cattle and water buffalo myoglobins |
title_short |
Muskox myoglobin: purification, characterization and kinetics studies compared with cattle and water buffalo myoglobins |
title_full |
Muskox myoglobin: purification, characterization and kinetics studies compared with cattle and water buffalo myoglobins |
title_fullStr |
Muskox myoglobin: purification, characterization and kinetics studies compared with cattle and water buffalo myoglobins |
title_full_unstemmed |
Muskox myoglobin: purification, characterization and kinetics studies compared with cattle and water buffalo myoglobins |
title_sort |
muskox myoglobin: purification, characterization and kinetics studies compared with cattle and water buffalo myoglobins |
publishDate |
2019 |
url |
https://hdl.handle.net/11591/414489 https://doi.org/10.1002/jsfa.9901 http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1097-0010 |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic muskox |
genre_facet |
Arctic muskox |
op_relation |
info:eu-repo/semantics/altIdentifier/pmid/31259416 info:eu-repo/semantics/altIdentifier/wos/WOS:000480439100001 volume:99 issue:14 firstpage:6278 lastpage:6286 numberofpages:9 journal:JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE https://hdl.handle.net/11591/414489 doi:10.1002/jsfa.9901 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-85070715800 http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1097-0010 |
op_doi |
https://doi.org/10.1002/jsfa.9901 |
container_title |
Journal of the Science of Food and Agriculture |
container_volume |
99 |
container_issue |
14 |
container_start_page |
6278 |
op_container_end_page |
6286 |
_version_ |
1796305725504356352 |