Influence of Proteolysis on the Binding Capacity of Flavor Compounds to Myofibrillar Proteins
Proteolysis occurs extensively during postmortem aging, enzymatic tenderization and fermentation of meat products, whereas less is understood regarding how proteolysis affects meat flavor. Myofibrillar proteins (MP) were extracted from beef longissimus dorsi muscle and subsequently treated with thre...
| Main Authors: | , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2022-03-01
|
| Series: | Foods |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2304-8158/11/6/891 |
| _version_ | 1827649068136923136 |
|---|---|
| author | Hao Li Rui Zheng Fangfang Zuo Chengyu Qian Zhengan Yao Ruipeng Dong Di Zhao Chunbao Li |
| author_facet | Hao Li Rui Zheng Fangfang Zuo Chengyu Qian Zhengan Yao Ruipeng Dong Di Zhao Chunbao Li |
| author_sort | Hao Li |
| collection | DOAJ |
| description | Proteolysis occurs extensively during postmortem aging, enzymatic tenderization and fermentation of meat products, whereas less is understood regarding how proteolysis affects meat flavor. Myofibrillar proteins (MP) were extracted from beef longissimus dorsi muscle and subsequently treated with three commercial proteases. The effect of proteolysis on the interactions between the treated MP and butyraldehyde, 2-pentanone, octanal and 2-octanone was investigated. The progress of proteolysis increased the degree of hydrolysis (DH) and the surface hydrophobicity but decreased the turbidity and particle size. Fluorescence-quenching analysis results indicated that the enzymatic treatment generally increased the quenching constant (K<sub>sv</sub>) between the treated MP and ketones but decreased the K<sub>sv</sub> between the treated MP and aldehydes, and the papain treatment changed the K<sub>sv</sub> value to a larger degree than treatment with proteinase K and bromelain. The adsorption assay showed that the proteinase K treatment largely increased the adsorption capacity of the MP to octanal (by 15.8–19.3%), whereas the bromelain treatment significantly reduced the adsorption capacity of the treated MP to butyraldehyde (by 6.0–7.9%) and 2-pentanone (by 9.7–11.9%). A correlation analysis demonstrated a strong positive correlation (0.859, <i>p</i> < 0.05) between the DH of the MP and the adsorption ability of the treated MP to octanal. This study highlighted the significant but complex influence of proteolysis on MP binding capacity to flavor compounds. |
| first_indexed | 2024-03-09T19:50:47Z |
| format | Article |
| id | doaj.art-f24ef2f1ecc9409f8d57cd7ca275950f |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-09T19:50:47Z |
| publishDate | 2022-03-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj.art-f24ef2f1ecc9409f8d57cd7ca275950f2023-11-24T01:11:33ZengMDPI AGFoods2304-81582022-03-0111689110.3390/foods11060891Influence of Proteolysis on the Binding Capacity of Flavor Compounds to Myofibrillar ProteinsHao Li0Rui Zheng1Fangfang Zuo2Chengyu Qian3Zhengan Yao4Ruipeng Dong5Di Zhao6Chunbao Li7College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaCollege of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaCollege of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaCollege of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaCollege of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaCollege of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaCollege of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaCollege of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaProteolysis occurs extensively during postmortem aging, enzymatic tenderization and fermentation of meat products, whereas less is understood regarding how proteolysis affects meat flavor. Myofibrillar proteins (MP) were extracted from beef longissimus dorsi muscle and subsequently treated with three commercial proteases. The effect of proteolysis on the interactions between the treated MP and butyraldehyde, 2-pentanone, octanal and 2-octanone was investigated. The progress of proteolysis increased the degree of hydrolysis (DH) and the surface hydrophobicity but decreased the turbidity and particle size. Fluorescence-quenching analysis results indicated that the enzymatic treatment generally increased the quenching constant (K<sub>sv</sub>) between the treated MP and ketones but decreased the K<sub>sv</sub> between the treated MP and aldehydes, and the papain treatment changed the K<sub>sv</sub> value to a larger degree than treatment with proteinase K and bromelain. The adsorption assay showed that the proteinase K treatment largely increased the adsorption capacity of the MP to octanal (by 15.8–19.3%), whereas the bromelain treatment significantly reduced the adsorption capacity of the treated MP to butyraldehyde (by 6.0–7.9%) and 2-pentanone (by 9.7–11.9%). A correlation analysis demonstrated a strong positive correlation (0.859, <i>p</i> < 0.05) between the DH of the MP and the adsorption ability of the treated MP to octanal. This study highlighted the significant but complex influence of proteolysis on MP binding capacity to flavor compounds.https://www.mdpi.com/2304-8158/11/6/891enzymatic hydrolysismyofibrillar proteinsflavor compounds |
| spellingShingle | Hao Li Rui Zheng Fangfang Zuo Chengyu Qian Zhengan Yao Ruipeng Dong Di Zhao Chunbao Li Influence of Proteolysis on the Binding Capacity of Flavor Compounds to Myofibrillar Proteins Foods enzymatic hydrolysis myofibrillar proteins flavor compounds |
| title | Influence of Proteolysis on the Binding Capacity of Flavor Compounds to Myofibrillar Proteins |
| title_full | Influence of Proteolysis on the Binding Capacity of Flavor Compounds to Myofibrillar Proteins |
| title_fullStr | Influence of Proteolysis on the Binding Capacity of Flavor Compounds to Myofibrillar Proteins |
| title_full_unstemmed | Influence of Proteolysis on the Binding Capacity of Flavor Compounds to Myofibrillar Proteins |
| title_short | Influence of Proteolysis on the Binding Capacity of Flavor Compounds to Myofibrillar Proteins |
| title_sort | influence of proteolysis on the binding capacity of flavor compounds to myofibrillar proteins |
| topic | enzymatic hydrolysis myofibrillar proteins flavor compounds |
| url | https://www.mdpi.com/2304-8158/11/6/891 |
| work_keys_str_mv | AT haoli influenceofproteolysisonthebindingcapacityofflavorcompoundstomyofibrillarproteins AT ruizheng influenceofproteolysisonthebindingcapacityofflavorcompoundstomyofibrillarproteins AT fangfangzuo influenceofproteolysisonthebindingcapacityofflavorcompoundstomyofibrillarproteins AT chengyuqian influenceofproteolysisonthebindingcapacityofflavorcompoundstomyofibrillarproteins AT zhenganyao influenceofproteolysisonthebindingcapacityofflavorcompoundstomyofibrillarproteins AT ruipengdong influenceofproteolysisonthebindingcapacityofflavorcompoundstomyofibrillarproteins AT dizhao influenceofproteolysisonthebindingcapacityofflavorcompoundstomyofibrillarproteins AT chunbaoli influenceofproteolysisonthebindingcapacityofflavorcompoundstomyofibrillarproteins |