Comparative Exploration of Antioxidant Properties of Alcalase- and Trypsin-Hydrolyzed Porcine By-Products and Their Classification for Industrial Use
Porcine by-products have garnered attention as an excellent material for producing antioxidant peptides; however, understanding the antioxidant characteristics of protein hydrolyzates derived from specific parts remains limited. In this study, we compared the antioxidant properties of protein hydrol...
Saved in:
Main Authors: | , , , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
MDPI AG
2024-12-01
|
Series: | Applied Sciences |
Subjects: | |
Online Access: | https://www.mdpi.com/2076-3417/15/1/47 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
_version_ | 1841549458975752192 |
---|---|
author | Jun Hwang Woo-Young Son Eun Ju Jeong Kyeong-Soo Kim Eui-Cheol Shin Dong-Heon Song Kyung-Woo Lee Hyun-Wook Kim |
author_facet | Jun Hwang Woo-Young Son Eun Ju Jeong Kyeong-Soo Kim Eui-Cheol Shin Dong-Heon Song Kyung-Woo Lee Hyun-Wook Kim |
author_sort | Jun Hwang |
collection | DOAJ |
description | Porcine by-products have garnered attention as an excellent material for producing antioxidant peptides; however, understanding the antioxidant characteristics of protein hydrolyzates derived from specific parts remains limited. In this study, we compared the antioxidant properties of protein hydrolyzates derived from major porcine organs (heart, kidney, spleen, liver, and lung) and performed classification based on their antioxidative potential. Their chemical composition exhibited significant variations, with a high protein content ranging from 15.90 to 20.30 g/100 g. Alcalase achieved higher hydrolysis efficiency than trypsin, which induced limited degradation of some proteins, such as porcine serum albumin. The hydrolyzates exhibited superior radical scavenging activities compared to the raw materials, although their reducing power remained unaffected or, in some instances, decreased. Hierarchical and k-mean cluster analyses revealed distinct antioxidant profiles and Alcalase-hydrolyzed kidney and trypsin-hydrolyzed lung hydrolyzates were deemed the most promising candidates, with strong radical scavenging activities and reducing power. Our findings indicate that, even when processed in bulk rather than being obtained from specific parts, porcine by-products can produce hydrolyzates rich in antioxidant peptides through enzymatic hydrolysis. However, selectively processing porcine kidneys with Alcalase and lungs with trypsin is recommended to produce premium products with enhanced and balanced antioxidant properties. |
format | Article |
id | doaj-art-a042b23307664856825c6adc78193f7e |
institution | Kabale University |
issn | 2076-3417 |
language | English |
publishDate | 2024-12-01 |
publisher | MDPI AG |
record_format | Article |
series | Applied Sciences |
spelling | doaj-art-a042b23307664856825c6adc78193f7e2025-01-10T13:14:16ZengMDPI AGApplied Sciences2076-34172024-12-011514710.3390/app15010047Comparative Exploration of Antioxidant Properties of Alcalase- and Trypsin-Hydrolyzed Porcine By-Products and Their Classification for Industrial UseJun Hwang0Woo-Young Son1Eun Ju Jeong2Kyeong-Soo Kim3Eui-Cheol Shin4Dong-Heon Song5Kyung-Woo Lee6Hyun-Wook Kim7Division of Animal Bioscience & Integrated Biotechnology, Gyeongsang National University, Jinju 52828, Republic of KoreaDivision of Animal Bioscience & Integrated Biotechnology, Gyeongsang National University, Jinju 52828, Republic of KoreaDepartment of Plant & Biomaterials Science, Gyeongsang National University, Jinju 52725, Republic of KoreaDepartment of Pharmaceutical Engineering, Gyeongsang National University, Jinju 52725, Republic of KoreaDepartment of GreenBio Science, Gyeongsang National University, Jinju 52725, Republic of KoreaAnimal Products Utilization Division, National Institute of Animal Science, Rural Development Administration, Wanju 55365, Republic of KoreaDepartment of Animal Science and Technology, Sanghuh College of Life Sciences, Konkuk University, Seoul 05029, Republic of KoreaDivision of Animal Bioscience & Integrated Biotechnology, Gyeongsang National University, Jinju 52828, Republic of KoreaPorcine by-products have garnered attention as an excellent material for producing antioxidant peptides; however, understanding the antioxidant characteristics of protein hydrolyzates derived from specific parts remains limited. In this study, we compared the antioxidant properties of protein hydrolyzates derived from major porcine organs (heart, kidney, spleen, liver, and lung) and performed classification based on their antioxidative potential. Their chemical composition exhibited significant variations, with a high protein content ranging from 15.90 to 20.30 g/100 g. Alcalase achieved higher hydrolysis efficiency than trypsin, which induced limited degradation of some proteins, such as porcine serum albumin. The hydrolyzates exhibited superior radical scavenging activities compared to the raw materials, although their reducing power remained unaffected or, in some instances, decreased. Hierarchical and k-mean cluster analyses revealed distinct antioxidant profiles and Alcalase-hydrolyzed kidney and trypsin-hydrolyzed lung hydrolyzates were deemed the most promising candidates, with strong radical scavenging activities and reducing power. Our findings indicate that, even when processed in bulk rather than being obtained from specific parts, porcine by-products can produce hydrolyzates rich in antioxidant peptides through enzymatic hydrolysis. However, selectively processing porcine kidneys with Alcalase and lungs with trypsin is recommended to produce premium products with enhanced and balanced antioxidant properties.https://www.mdpi.com/2076-3417/15/1/47cluster analysisporcine offalporcine serum albuminprotein solubility |
spellingShingle | Jun Hwang Woo-Young Son Eun Ju Jeong Kyeong-Soo Kim Eui-Cheol Shin Dong-Heon Song Kyung-Woo Lee Hyun-Wook Kim Comparative Exploration of Antioxidant Properties of Alcalase- and Trypsin-Hydrolyzed Porcine By-Products and Their Classification for Industrial Use Applied Sciences cluster analysis porcine offal porcine serum albumin protein solubility |
title | Comparative Exploration of Antioxidant Properties of Alcalase- and Trypsin-Hydrolyzed Porcine By-Products and Their Classification for Industrial Use |
title_full | Comparative Exploration of Antioxidant Properties of Alcalase- and Trypsin-Hydrolyzed Porcine By-Products and Their Classification for Industrial Use |
title_fullStr | Comparative Exploration of Antioxidant Properties of Alcalase- and Trypsin-Hydrolyzed Porcine By-Products and Their Classification for Industrial Use |
title_full_unstemmed | Comparative Exploration of Antioxidant Properties of Alcalase- and Trypsin-Hydrolyzed Porcine By-Products and Their Classification for Industrial Use |
title_short | Comparative Exploration of Antioxidant Properties of Alcalase- and Trypsin-Hydrolyzed Porcine By-Products and Their Classification for Industrial Use |
title_sort | comparative exploration of antioxidant properties of alcalase and trypsin hydrolyzed porcine by products and their classification for industrial use |
topic | cluster analysis porcine offal porcine serum albumin protein solubility |
url | https://www.mdpi.com/2076-3417/15/1/47 |
work_keys_str_mv | AT junhwang comparativeexplorationofantioxidantpropertiesofalcalaseandtrypsinhydrolyzedporcinebyproductsandtheirclassificationforindustrialuse AT wooyoungson comparativeexplorationofantioxidantpropertiesofalcalaseandtrypsinhydrolyzedporcinebyproductsandtheirclassificationforindustrialuse AT eunjujeong comparativeexplorationofantioxidantpropertiesofalcalaseandtrypsinhydrolyzedporcinebyproductsandtheirclassificationforindustrialuse AT kyeongsookim comparativeexplorationofantioxidantpropertiesofalcalaseandtrypsinhydrolyzedporcinebyproductsandtheirclassificationforindustrialuse AT euicheolshin comparativeexplorationofantioxidantpropertiesofalcalaseandtrypsinhydrolyzedporcinebyproductsandtheirclassificationforindustrialuse AT dongheonsong comparativeexplorationofantioxidantpropertiesofalcalaseandtrypsinhydrolyzedporcinebyproductsandtheirclassificationforindustrialuse AT kyungwoolee comparativeexplorationofantioxidantpropertiesofalcalaseandtrypsinhydrolyzedporcinebyproductsandtheirclassificationforindustrialuse AT hyunwookkim comparativeexplorationofantioxidantpropertiesofalcalaseandtrypsinhydrolyzedporcinebyproductsandtheirclassificationforindustrialuse |