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Critical Factors of Reacquainting Consumer Trust in E-Commerce
FAN, Mingyue,AMMAH, Victoria,DAKHAN, Sarfraz Ahmed,LIU, Ran,MINGLE, Moses NiiAkwei,PU, Zhengjia Korea Distribution Science Association 2021 The Journal of Asian Finance, Economics and Busine Vol.8 No.3
Knowing how to build and maintain consumer trust is crucial for e-commerce. Despite the number of empirical studies that have explored the factors that influence consumer trust, none of them considers the relative importance of different antecedents and how they interact to influence consumer trust. Therefore, based on the integrated Decision Making Trial and Evaluation Laboratory (DEMATEL) and Interpretive Structural Modeling (ISM) approaches, we establish a hierarchical structural model, which not only demonstrates the intensity of the relationships but also identifies the interdependence among the drivers of consumer trust in E-commerce. The findings confirm that propensity to trust is the most important determinant of consumer trust. The brand-related factors and platform-related factors are prominent in the process of building trust as they influence consumer trust indirectly through propensity to trust. Geographic location, demographic variables, and high security are identified as the root causes that affect consumer trust through other trust antecedents. Furthermore, the findings of this study offer valuable insights into an important element of e-commerce and provide a useful platform for future research. More represented samples and factors are encouraged for further research to ensure research fairness and minimize consumer distrust and uncertainty.
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Cong Guilong,Li Mingyu,Dong Sitong,Ai Teng,Ren Xiaopeng,Li Xianzhen,Wang Conggang,Yang Fan 한국응용생명화학회 2024 Applied Biological Chemistry (Appl Biol Chem) Vol.67 No.-
Maltotetraose amylase (Mta) catalyzes the hydrolysis of amylaceous polysaccharides into maltotetraose, which is an important functional sugar used in the food industry. However, the lack of efficient expression systems for recombinant Mta has hindered its scale-up production and application. In this study, a codon-optimized mta gene from Pseudomonas saccharophila was efficiently produced in Bacillus subtilis by optimizing the regulatory elements. First, a plasmid library containing 173 different signal peptide sequences placed upstream of mta gene was constructed, and transformed into B. subtilis strain WB800N( amyE Δ1) for high-throughput screening. The signal peptide yhcR was found to significantly enhance the secretion of Mta, reaching an activity of 75.4 U/mL in the culture medium. After optimization of the promoters, the Mta activity was further increased to 100.3 U/mL using a dual-promoter P HpaII P amyE . Finally, the carbon sources and nitrogen sources for recombinant Mta production were optimized, yielding a highest Mta activity of 288.9 U/mL under the optimal culture conditions. The crude enzyme solution containing recombinant Mta produced a highest maltotetraose yield of 70.3% with 200 g/L of maltodextrin as the substrate. Therefore, the present study have demonstrated a high yield of Mta produced in B. subtilis , laying the foundation for large-scale Mta production and application. Maltotetraose amylase (Mta) catalyzes the hydrolysis of amylaceous polysaccharides into maltotetraose, which is an important functional sugar used in the food industry. However, the lack of efficient expression systems for recombinant Mta has hindered its scale-up production and application. In this study, a codon-optimized mta gene from Pseudomonas saccharophila was efficiently produced in Bacillus subtilis by optimizing the regulatory elements. First, a plasmid library containing 173 different signal peptide sequences placed upstream of mta gene was constructed, and transformed into B. subtilis strain WB800N(amyEΔ1) for high-throughput screening. The signal peptide yhcR was found to significantly enhance the secretion of Mta, reaching an activity of 75.4 U/mL in the culture medium. After optimization of the promoters, the Mta activity was further increased to 100.3 U/mL using a dual-promoter PHpaIIPamyE. Finally, the carbon sources and nitrogen sources for recombinant Mta production were optimized, yielding a highest Mta activity of 288.9 U/mL under the optimal culture conditions. The crude enzyme solution containing recombinant Mta produced a highest maltotetraose yield of 70.3% with 200 g/L of maltodextrin as the substrate. Therefore, the present study have demonstrated a high yield of Mta produced in B. subtilis, laying the foundation for large-scale Mta production and application.
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