To develop an effective surface proteomic profiling method for Gram-negative bacteria, whose thin cell walls make them prone to cytoplasmic protein leakage, Zeolitic imidazolate framework-8 (ZIF-8) with varying degrees of degradation was used as a porous protective exoskeleton for live cells, thereby helping maintain cell morphology and physiological activity under stressful conditions. We optimized a one-pot method to synthesize ZIF-8 protective shells onto the Vibrio parahaemolyticus (VP) surface using zinc acetate and dimethyl imidazole and characterized ZIF-8 degradation kinetics under acidic PBS or EDTA treatment. A rapid and controllable method for ZIF-8 degradation and analysis was developed. Scanning electron microscopy (SEM) and energydispersive X-ray spectroscopy (EDS) revealed 99.99% VP encapsulation efficiency by ZIF-8. PBS at pH 5.0 could achieve controlled degradation of the ZIF-8 protective shell in 30 minutes, with a maximum degradation rate of 80.83%. In contrast, 50 mmol•L-1 EDTA could degrade the shell in 15 minutes, with a maximum degradation rate of 96.00%. Observation via microscopy after lysozyme digestion and ultrapure water treatment showed that cells encapsulated with ZIF-8 and subsequently degraded by EDTA or PBS could maintain cell integrity in lysozyme-treated and low osmotic pressure environments. BCA protein quantification showed that cytoplasmic protein leakage reduced by 95.16% and 94.47% after ZIF-8 encapsulation and degradation by PBS or EDTA, respectively. ZIF-8 encapsulation followed by controlled degradation creates an exoskeleton for Vibrio parahaemolyticus, effectively protecting cell morphology and reducing cytoplasmic protein leakage. These findings provide a reference method to facilitate application of surface proteome analysis for discovery of immune detection targets and vaccine development.