Heterologous Expression of the <i>Lactobacillus sakei</i> Multiple Copper Oxidase to Degrade Histamine and Tyramine at Different Environmental Conditions
Biogenic amines (BAs) are produced by microbial decarboxylation in various foods. Histamine and tyramine are recognized as the most toxic of all BAs. Applying degrading amine enzymes such as multicopper oxidase (MCO) is considered an effective method to reduce BAs in food systems. This study analyze...
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MDPI AG
2022-10-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/11/20/3306 |
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| author | Xiaofu Wang Yunsong Zhao Sufang Zhang Xinping Lin Huipeng Liang Yingxi Chen Chaofan Ji |
| author_facet | Xiaofu Wang Yunsong Zhao Sufang Zhang Xinping Lin Huipeng Liang Yingxi Chen Chaofan Ji |
| author_sort | Xiaofu Wang |
| collection | DOAJ |
| description | Biogenic amines (BAs) are produced by microbial decarboxylation in various foods. Histamine and tyramine are recognized as the most toxic of all BAs. Applying degrading amine enzymes such as multicopper oxidase (MCO) is considered an effective method to reduce BAs in food systems. This study analyzed the characterization of heterologously expressed MCO from <i>L. sakei</i> LS. Towards the typical substrate 2,2′-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), the optimal temperature and pH for recombinant MCO (rMCO) were 25 °C and 3.0, respectively, with the specific enzyme activity of 1.27 U/mg. Then, the effect of different environmental factors on the degrading activity of MCO towards two kinds of BAs was investigated. The degradation activity of rMCO is independent of exogenous copper and mediators. Additionally, the oxidation ability of rMCO was improved for histamine and tyramine with an increased NaCl concentration. Several food matrices could influence the amine-oxidizing activity of rMCO. Although the histamine-degrading activities of rMCO were affected, this enzyme reached a degradation rate of 28.1% in the presence of surimi. Grape juice improved the tyramine degradation activity of rMCO by up to 31.18%. These characteristics of rMCO indicate that this enzyme would be a good candidate for degrading toxic biogenic amines in food systems. |
| first_indexed | 2024-03-09T03:38:18Z |
| format | Article |
| id | doaj.art-47272787669a47bb80859c2a3d6cb593 |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-09T03:38:18Z |
| publishDate | 2022-10-01 |
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| record_format | Article |
| series | Foods |
| spelling | doaj.art-47272787669a47bb80859c2a3d6cb5932023-12-03T14:44:06ZengMDPI AGFoods2304-81582022-10-011120330610.3390/foods11203306Heterologous Expression of the <i>Lactobacillus sakei</i> Multiple Copper Oxidase to Degrade Histamine and Tyramine at Different Environmental ConditionsXiaofu Wang0Yunsong Zhao1Sufang Zhang2Xinping Lin3Huipeng Liang4Yingxi Chen5Chaofan Ji6School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, ChinaSchool of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, ChinaSchool of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, ChinaSchool of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, ChinaSchool of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, ChinaSchool of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, ChinaSchool of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, ChinaBiogenic amines (BAs) are produced by microbial decarboxylation in various foods. Histamine and tyramine are recognized as the most toxic of all BAs. Applying degrading amine enzymes such as multicopper oxidase (MCO) is considered an effective method to reduce BAs in food systems. This study analyzed the characterization of heterologously expressed MCO from <i>L. sakei</i> LS. Towards the typical substrate 2,2′-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), the optimal temperature and pH for recombinant MCO (rMCO) were 25 °C and 3.0, respectively, with the specific enzyme activity of 1.27 U/mg. Then, the effect of different environmental factors on the degrading activity of MCO towards two kinds of BAs was investigated. The degradation activity of rMCO is independent of exogenous copper and mediators. Additionally, the oxidation ability of rMCO was improved for histamine and tyramine with an increased NaCl concentration. Several food matrices could influence the amine-oxidizing activity of rMCO. Although the histamine-degrading activities of rMCO were affected, this enzyme reached a degradation rate of 28.1% in the presence of surimi. Grape juice improved the tyramine degradation activity of rMCO by up to 31.18%. These characteristics of rMCO indicate that this enzyme would be a good candidate for degrading toxic biogenic amines in food systems.https://www.mdpi.com/2304-8158/11/20/3306<i>Lactobacillus sakei</i>biodegradationmulticopper oxidasefood matricesbiogenic amines |
| spellingShingle | Xiaofu Wang Yunsong Zhao Sufang Zhang Xinping Lin Huipeng Liang Yingxi Chen Chaofan Ji Heterologous Expression of the <i>Lactobacillus sakei</i> Multiple Copper Oxidase to Degrade Histamine and Tyramine at Different Environmental Conditions Foods <i>Lactobacillus sakei</i> biodegradation multicopper oxidase food matrices biogenic amines |
| title | Heterologous Expression of the <i>Lactobacillus sakei</i> Multiple Copper Oxidase to Degrade Histamine and Tyramine at Different Environmental Conditions |
| title_full | Heterologous Expression of the <i>Lactobacillus sakei</i> Multiple Copper Oxidase to Degrade Histamine and Tyramine at Different Environmental Conditions |
| title_fullStr | Heterologous Expression of the <i>Lactobacillus sakei</i> Multiple Copper Oxidase to Degrade Histamine and Tyramine at Different Environmental Conditions |
| title_full_unstemmed | Heterologous Expression of the <i>Lactobacillus sakei</i> Multiple Copper Oxidase to Degrade Histamine and Tyramine at Different Environmental Conditions |
| title_short | Heterologous Expression of the <i>Lactobacillus sakei</i> Multiple Copper Oxidase to Degrade Histamine and Tyramine at Different Environmental Conditions |
| title_sort | heterologous expression of the i lactobacillus sakei i multiple copper oxidase to degrade histamine and tyramine at different environmental conditions |
| topic | <i>Lactobacillus sakei</i> biodegradation multicopper oxidase food matrices biogenic amines |
| url | https://www.mdpi.com/2304-8158/11/20/3306 |
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