Expression and Thermal Stability Analysis of Shark Single Domain Antibody-Alkaline Phosphatase Fusion Protein

LIU Xin; QU Yue-kuan; CAO Li-min; SUI Jian-xin

doi:10.13386/j.issn1002-0306.2020020051

Volume 41 Issue 21

Oct. 2020

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Science and Technology of Food Industry > 2020 > 41(21): 110-115. > DOI: 10.13386/j.issn1002-0306.2020020051

LIU Xin, QU Yue-kuan, CAO Li-min, SUI Jian-xin. Expression and Thermal Stability Analysis of Shark Single Domain Antibody-Alkaline Phosphatase Fusion Protein[J]. Science and Technology of Food Industry, 2020, 41(21): 110-115. DOI: 10.13386/j.issn1002-0306.2020020051

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Expression and Thermal Stability Analysis of Shark Single Domain Antibody-Alkaline Phosphatase Fusion Protein

College of Food Science and Engineering, Ocean University of China, Qingdao 266003, China

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Received Date: February 06, 2020
Available Online: November 11, 2020

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The stability of enzyme-labeled antibody plays an important role in enzyme-linked immunosorbent assay(ELISA),but the disadvantages in thermal stability of the conventional antibody-enzyme conjugation has restricted the application of enzyme-labeled antibodies in ELISA. In this study,the shark single domain antibody specific to myofibrillar-binding serine protease(MBSP)fused with alkaline phosphatase was expressed and its affinity and thermal stability were investigated. Results showed that when induced with Isopropyl-beta-D-thiogalactopyranoside(IPTG)at 16 ℃,the fusion protein which was about 63 kDa in molecular weight,which could be expressed in soluble with high affinity and thermal stability. The K_D value of the fusion protein to MBSP could reach 7.80×10^-8 mol/L and the binding activity of fusion protein could be kept well when treated at 58 ℃ even for 180 minutes. All the results implied that the fusion protein could be used as a potential immunodiagnostic agent in ELISA.
- shark single domain antibody,
- alkaline phosphatase,
- fusion protein,
- affinity,
- thermal stability

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