Purification and Characterization of Pancreatic Carboxypeptidase A1 (CBPA1) of bovine (Bos taurus) and sheep (Ovis aries) for Potential Application as Halal Enzymes.

Purification and Characterization of Pancreatic Carboxypeptidase A1 (CBPA1) of bovine (Bos taurus) and sheep (Ovis aries) for Potential Application as Halal Enzymes.

Background: Carboxypeptidase A1 (CBPA1) is a well-known protease pancreatic enzyme family member. It catalyzes the hydrolysis of the carbonyl-terminal residue from peptide or ester substrates by cleavage of the peptide or ester bond. Objective: This study aimed to purify and characterize CBPA1 from...

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Published in:Journal of Pancreatology
Main Author: Reshidan H.B.; Jonet M.A.B.; Ariffin Z.B.Z.; Hamid U.M.B.A.
Format: Article
Language:English
Published: Wolters Kluwer Health 2024
Online Access:https://www.scopus.com/inward/record.uri?eid=2-s2.0-85212404337&doi=10.1097%2fJP9.0000000000000208&partnerID=40&md5=4c0f6d2d982129759fd52fa8542a71b6
id 2-s2.0-85212404337
spelling 2-s2.0-85212404337
Reshidan H.B.; Jonet M.A.B.; Ariffin Z.B.Z.; Hamid U.M.B.A.
Purification and Characterization of Pancreatic Carboxypeptidase A1 (CBPA1) of bovine (Bos taurus) and sheep (Ovis aries) for Potential Application as Halal Enzymes.
2024
Journal of Pancreatology


10.1097/JP9.0000000000000208
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85212404337&doi=10.1097%2fJP9.0000000000000208&partnerID=40&md5=4c0f6d2d982129759fd52fa8542a71b6
Background: Carboxypeptidase A1 (CBPA1) is a well-known protease pancreatic enzyme family member. It catalyzes the hydrolysis of the carbonyl-terminal residue from peptide or ester substrates by cleavage of the peptide or ester bond. Objective: This study aimed to purify and characterize CBPA1 from bovine (Bos taurus) and sheep (Ovis aries) fresh pancreatic tissue. Methods: Bovine and sheep pancreas were collected freshly from Abattoir Complex, Department of Veterinary Services, Shah Alam. The fats were removed by trimming grossly visible fat and by extraction using organic solvents. The CBPA1 was further purified by anion exchange and gel filtration chromatography. Protein identification was performed via LC-MS/MS (liquid chromatography-mass spectrometry). The proteolytic activity was measured using protease assay. Results: Successful purification of CBPA1 from bovine and sheep was visualized as single protein bands on sodium dodecyl sulphate-polyacrylamide gel, which LC-MS/MS confirmed as CBPA1 with the molecular mass of 47.05kDa and 46.87kDa for bovine (Accession number – P00730) and sheep (Accession number – W5P5N4), respectively. The proteolytic enzyme activity was confirmed with protease assay whereby bovine CBPA1 showed higher protease activity than sheep. Conclusion: In conclusion, bovine and sheep CBPA1 were successfully purified from fresh pancreatic tissue and may have the potential for further applications as the proteolytic activity recorded was comparable to that of the porcine protease. Copyright © 2024 The Chinese Medical Association, Published by Wolters Kluwer Health, Inc.
Wolters Kluwer Health
20965664
English
Article
All Open Access; Gold Open Access
author Reshidan H.B.; Jonet M.A.B.; Ariffin Z.B.Z.; Hamid U.M.B.A.
spellingShingle Reshidan H.B.; Jonet M.A.B.; Ariffin Z.B.Z.; Hamid U.M.B.A.
Purification and Characterization of Pancreatic Carboxypeptidase A1 (CBPA1) of bovine (Bos taurus) and sheep (Ovis aries) for Potential Application as Halal Enzymes.
author_facet Reshidan H.B.; Jonet M.A.B.; Ariffin Z.B.Z.; Hamid U.M.B.A.
author_sort Reshidan H.B.; Jonet M.A.B.; Ariffin Z.B.Z.; Hamid U.M.B.A.
title Purification and Characterization of Pancreatic Carboxypeptidase A1 (CBPA1) of bovine (Bos taurus) and sheep (Ovis aries) for Potential Application as Halal Enzymes.
title_short Purification and Characterization of Pancreatic Carboxypeptidase A1 (CBPA1) of bovine (Bos taurus) and sheep (Ovis aries) for Potential Application as Halal Enzymes.
title_full Purification and Characterization of Pancreatic Carboxypeptidase A1 (CBPA1) of bovine (Bos taurus) and sheep (Ovis aries) for Potential Application as Halal Enzymes.
title_fullStr Purification and Characterization of Pancreatic Carboxypeptidase A1 (CBPA1) of bovine (Bos taurus) and sheep (Ovis aries) for Potential Application as Halal Enzymes.
title_full_unstemmed Purification and Characterization of Pancreatic Carboxypeptidase A1 (CBPA1) of bovine (Bos taurus) and sheep (Ovis aries) for Potential Application as Halal Enzymes.
title_sort Purification and Characterization of Pancreatic Carboxypeptidase A1 (CBPA1) of bovine (Bos taurus) and sheep (Ovis aries) for Potential Application as Halal Enzymes.
publishDate 2024
container_title Journal of Pancreatology
container_volume
container_issue
doi_str_mv 10.1097/JP9.0000000000000208
url https://www.scopus.com/inward/record.uri?eid=2-s2.0-85212404337&doi=10.1097%2fJP9.0000000000000208&partnerID=40&md5=4c0f6d2d982129759fd52fa8542a71b6
description Background: Carboxypeptidase A1 (CBPA1) is a well-known protease pancreatic enzyme family member. It catalyzes the hydrolysis of the carbonyl-terminal residue from peptide or ester substrates by cleavage of the peptide or ester bond. Objective: This study aimed to purify and characterize CBPA1 from bovine (Bos taurus) and sheep (Ovis aries) fresh pancreatic tissue. Methods: Bovine and sheep pancreas were collected freshly from Abattoir Complex, Department of Veterinary Services, Shah Alam. The fats were removed by trimming grossly visible fat and by extraction using organic solvents. The CBPA1 was further purified by anion exchange and gel filtration chromatography. Protein identification was performed via LC-MS/MS (liquid chromatography-mass spectrometry). The proteolytic activity was measured using protease assay. Results: Successful purification of CBPA1 from bovine and sheep was visualized as single protein bands on sodium dodecyl sulphate-polyacrylamide gel, which LC-MS/MS confirmed as CBPA1 with the molecular mass of 47.05kDa and 46.87kDa for bovine (Accession number – P00730) and sheep (Accession number – W5P5N4), respectively. The proteolytic enzyme activity was confirmed with protease assay whereby bovine CBPA1 showed higher protease activity than sheep. Conclusion: In conclusion, bovine and sheep CBPA1 were successfully purified from fresh pancreatic tissue and may have the potential for further applications as the proteolytic activity recorded was comparable to that of the porcine protease. Copyright © 2024 The Chinese Medical Association, Published by Wolters Kluwer Health, Inc.
publisher Wolters Kluwer Health
issn 20965664
language English
format Article
accesstype All Open Access; Gold Open Access
record_format scopus
collection Scopus
_version_ 1820775436647399424

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