Abstract

The anti-tumor effect of aconitine in melanoma cell line B16 has been studied in this paper. We found that B16 cells showed significantly reduced growth rates and increased apoptotic effects in the presence of aconitine. Furthermore, aconitine inhibited the PI3K/AKT and MAPK/ERK1/2 signaling pathways, thus regulating the levels of protein and mRNA of PCNA and apoptotic related signaling molecules. Above all, we found that aconitine showed an anti-melanoma effect in suppressing tumor growth in vivo. In conclusion, we show that aconitine may be a useful anticancer drug in the future.

Highlights

  • Biocatalysts are extensively used in the industrial production of bulk chemicals and pharmaceuticals, and over 300 processes have already been implemented [1]

  • Immobilization of β-galactosidase from E. coli and Kluyveromyces lactis on thiolsulphinate-agarose and glutaraldehyde-agarose clearly demonstrates the relation between the number of bonds formed between the enzyme and the carrier and enzyme activity [168]

  • Yilmaz et al (2011) reported that sporopollenin-based encapsulated lipase in particular had higher conversion and enantioselectivity compared to sol–gel free lipase [186]. These results reveal that sol–gel encapsulated lipase has high enantioselectivity (E) and conversion (x) compared with covalently immobilized lipase (Candida rugosa lipase)

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Summary

Introduction

Biocatalysts are extensively used in the industrial production of bulk chemicals and pharmaceuticals, and over 300 processes have already been implemented [1]. For a given biocatalytic process, the native enzyme does not meet the requirements for large-scale application, and its properties need to be optimized or modulated Many industrial enzymes, such as lipases, with a wide range of substrate specificities, are utilized in many processes, often compromising the desired productivity. The role of protein engineering is to overcome the limitations of natural enzymes as biocatalysts and engineer process-specific biocatalysts This includes optimizing the chemoselectivity, regioselectivity, and, especially, stereoselectivity of the biocatalyst, as well as process-related aspects, such as long-term stability at certain temperatures or pH-values and activity in the presence of high substrate concentrations to achieve maximal productivity. This review covers different strategies of protein engineering and immobilization to modulate the properties of enzymes to suit industrial processes

Protein Engineering to Upgrade Industrial Enzymes
Method
Activity
Thermal Stability
Solvent Stability
Substrate Specificity
A Way Forward
Immobilization to Upgrade Industrial Enzymes
Selectivity
Substrate Tolerance
Multi-Step Reactions
Advances in Enzyme Immobilization
New Technology for Enzyme Immobilization
Microwave Irradiation
Photoimmobilization Technology
Enzymatic Immobilization of Enzyme
Recommendation for the Future of Immobilization Technology
Integration of Different Techniques
Findings
Conclusions
Full Text
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