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
Citation: 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

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

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  • Received Date: February 06, 2020
  • Available Online: November 11, 2020
  • 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 KD 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.
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