In vitro assembly of the trehalose bi-enzyme complex with artificial scaffold protein
Introduction: Trehalose is a significant rare sugar known for its stable properties and ability to protect biomolecules from environmental factors.Methods: In this study, we present a novel approach utilizing a scaffold protein-mediated assembly method for the formation of a trehalose bi-enzyme comp...
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| Format: | Article |
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Frontiers Media S.A.
2023-08-01
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| Series: | Frontiers in Bioengineering and Biotechnology |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fbioe.2023.1251298/full |
| _version_ | 1827855930057818112 |
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| author | Xiangyi Wang Xiangyi Wang Yi Jiang Yi Jiang Hongling Liu Hongling Liu Xinyi Zhang Xinyi Zhang Haibo Yuan Haibo Yuan Di Huang Di Huang Tengfei Wang Tengfei Wang |
| author_facet | Xiangyi Wang Xiangyi Wang Yi Jiang Yi Jiang Hongling Liu Hongling Liu Xinyi Zhang Xinyi Zhang Haibo Yuan Haibo Yuan Di Huang Di Huang Tengfei Wang Tengfei Wang |
| author_sort | Xiangyi Wang |
| collection | DOAJ |
| description | Introduction: Trehalose is a significant rare sugar known for its stable properties and ability to protect biomolecules from environmental factors.Methods: In this study, we present a novel approach utilizing a scaffold protein-mediated assembly method for the formation of a trehalose bi-enzyme complex. This complex consists of maltooligosyltrehalose synthase (MTSase) and maltooligosyltrehalose trehalohydrolase (MTHase), which work in tandem to catalyze the substrate and enhance the overall catalytic efficiency. Utilizing the specific interaction between cohesin and dockerin, this study presents the implementation of an assembly, an analysis of its efficiency, and an exploration of strategies to enhance enzyme utilization through the construction of a bi-enzyme complex under optimal conditions in vitro.Results and Discussion: The bi-enzyme complex demonstrated a trehalose production level 1.5 times higher than that of the free enzyme mixture at 40 h, with a sustained upward trend. Compared to free enzyme mixtures, the adoption of a scaffold protein-mediated bi-enzyme complex may improve cascade reactions and catalytic effects, thus presenting promising prospects. |
| first_indexed | 2024-03-12T12:17:44Z |
| format | Article |
| id | doaj.art-9c3e27182bcd4412a7421b2f5dd6dc01 |
| institution | Directory Open Access Journal |
| issn | 2296-4185 |
| language | English |
| last_indexed | 2024-03-12T12:17:44Z |
| publishDate | 2023-08-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Bioengineering and Biotechnology |
| spelling | doaj.art-9c3e27182bcd4412a7421b2f5dd6dc012023-08-30T08:51:12ZengFrontiers Media S.A.Frontiers in Bioengineering and Biotechnology2296-41852023-08-011110.3389/fbioe.2023.12512981251298In vitro assembly of the trehalose bi-enzyme complex with artificial scaffold proteinXiangyi Wang0Xiangyi Wang1Yi Jiang2Yi Jiang3Hongling Liu4Hongling Liu5Xinyi Zhang6Xinyi Zhang7Haibo Yuan8Haibo Yuan9Di Huang10Di Huang11Tengfei Wang12Tengfei Wang13State Key Laboratory of Biobased Material and Green Papermaking (LBMP), Shandong Academy of Sciences, Qilu University of Technology, Jinan, Shandong, ChinaKey Laboratory of Shandong Microbial Engineering, School of Bioengineering, Shandong Academy of Sciences, Qilu University of Technology, Jinan, Shandong, ChinaState Key Laboratory of Biobased Material and Green Papermaking (LBMP), Shandong Academy of Sciences, Qilu University of Technology, Jinan, Shandong, ChinaKey Laboratory of Shandong Microbial Engineering, School of Bioengineering, Shandong Academy of Sciences, Qilu University of Technology, Jinan, Shandong, ChinaState Key Laboratory of Biobased Material and Green Papermaking (LBMP), Shandong Academy of Sciences, Qilu University of Technology, Jinan, Shandong, ChinaKey Laboratory of Shandong Microbial Engineering, School of Bioengineering, Shandong Academy of Sciences, Qilu University of Technology, Jinan, Shandong, ChinaState Key Laboratory of Biobased Material and Green Papermaking (LBMP), Shandong Academy of Sciences, Qilu University of Technology, Jinan, Shandong, ChinaKey Laboratory of Shandong Microbial Engineering, School of Bioengineering, Shandong Academy of Sciences, Qilu University of Technology, Jinan, Shandong, ChinaState Key Laboratory of Biobased Material and Green Papermaking (LBMP), Shandong Academy of Sciences, Qilu University of Technology, Jinan, Shandong, ChinaKey Laboratory of Shandong Microbial Engineering, School of Bioengineering, Shandong Academy of Sciences, Qilu University of Technology, Jinan, Shandong, ChinaState Key Laboratory of Biobased Material and Green Papermaking (LBMP), Shandong Academy of Sciences, Qilu University of Technology, Jinan, Shandong, ChinaKey Laboratory of Shandong Microbial Engineering, School of Bioengineering, Shandong Academy of Sciences, Qilu University of Technology, Jinan, Shandong, ChinaState Key Laboratory of Biobased Material and Green Papermaking (LBMP), Shandong Academy of Sciences, Qilu University of Technology, Jinan, Shandong, ChinaKey Laboratory of Shandong Microbial Engineering, School of Bioengineering, Shandong Academy of Sciences, Qilu University of Technology, Jinan, Shandong, ChinaIntroduction: Trehalose is a significant rare sugar known for its stable properties and ability to protect biomolecules from environmental factors.Methods: In this study, we present a novel approach utilizing a scaffold protein-mediated assembly method for the formation of a trehalose bi-enzyme complex. This complex consists of maltooligosyltrehalose synthase (MTSase) and maltooligosyltrehalose trehalohydrolase (MTHase), which work in tandem to catalyze the substrate and enhance the overall catalytic efficiency. Utilizing the specific interaction between cohesin and dockerin, this study presents the implementation of an assembly, an analysis of its efficiency, and an exploration of strategies to enhance enzyme utilization through the construction of a bi-enzyme complex under optimal conditions in vitro.Results and Discussion: The bi-enzyme complex demonstrated a trehalose production level 1.5 times higher than that of the free enzyme mixture at 40 h, with a sustained upward trend. Compared to free enzyme mixtures, the adoption of a scaffold protein-mediated bi-enzyme complex may improve cascade reactions and catalytic effects, thus presenting promising prospects.https://www.frontiersin.org/articles/10.3389/fbioe.2023.1251298/fulltrehaloseartificial scaffold proteinfusion enzymebi-enzyme complexcascade enzyme reactionsubstrate channel effect |
| spellingShingle | Xiangyi Wang Xiangyi Wang Yi Jiang Yi Jiang Hongling Liu Hongling Liu Xinyi Zhang Xinyi Zhang Haibo Yuan Haibo Yuan Di Huang Di Huang Tengfei Wang Tengfei Wang In vitro assembly of the trehalose bi-enzyme complex with artificial scaffold protein Frontiers in Bioengineering and Biotechnology trehalose artificial scaffold protein fusion enzyme bi-enzyme complex cascade enzyme reaction substrate channel effect |
| title | In vitro assembly of the trehalose bi-enzyme complex with artificial scaffold protein |
| title_full | In vitro assembly of the trehalose bi-enzyme complex with artificial scaffold protein |
| title_fullStr | In vitro assembly of the trehalose bi-enzyme complex with artificial scaffold protein |
| title_full_unstemmed | In vitro assembly of the trehalose bi-enzyme complex with artificial scaffold protein |
| title_short | In vitro assembly of the trehalose bi-enzyme complex with artificial scaffold protein |
| title_sort | in vitro assembly of the trehalose bi enzyme complex with artificial scaffold protein |
| topic | trehalose artificial scaffold protein fusion enzyme bi-enzyme complex cascade enzyme reaction substrate channel effect |
| url | https://www.frontiersin.org/articles/10.3389/fbioe.2023.1251298/full |
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