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Jang, B.B., Lee, K.P., Dalhee Min, A. and Suh, J. (1999) Immobile Artificial Metalloproteinase Containing Both Catalytic and Binding Groups. J.Am.Chem.SOC, 120, 12008-12016. https://doi.org/10.1021/ja981723

has been cited by the following article:

• TITLE: MOFzyme: FJU-21 with Intrinsic High Protease-Like Activity for Hydrolysis of Proteins

  AUTHORS: Lingli Li, Bin Li, Daomei Chen, Jingchen Zhao, Dongqi Yang, Danhua Ma, Liang Jiang, Yepeng Yang, Yizhou Li, Jiaqiang Wang

  KEYWORDS: Metal-Organic Frameworks (MOFs), FJU-21, Protease Mimetics, Reusability

  JOURNAL NAME: Journal of Biosciences and Medicines, Vol.7 No.5, May 31, 2019

  ABSTRACT: In this work, metal-organic frameworks (MOFs) FJU-21 was synthesized by solvothermal method. The crystal structure of FJU-21 was characterized by XRD and BET and it was applied to the catalytic hydrolysis of bovine serum albumin. The effects of reaction pH, temperature and reaction time on the catalytic activity of FJU-21 were studied. FJU-21 were found to possess an intrinsic enzyme mimicking activity similar to that found in trypsin. The Michaelis constant (Km) of the artificial protease (0.18 × 10-3 - 0.20 × 10-3 M-1) was about 15-fold lower than that free trypsin (2.7 × 10-3 M-1) and about 3-fold lower than that of soluble Cu(II) oxacyclen (0.54 × 10-3 M-1). The Kcat of FJU-21 is 102 times higher than that of soluble Cu(II) oxacyclen catalysts and, indicating a much higher affinity of BSA for FJU-21 surface. FJU-21 could be reused for eleven times without losing in its activity.