A newly moderate halophile Halobacillus sp. LY4 producing extracellular amylase and protease was isolated and identified. Production of both enzymes was synchronized with bacterial growth and reached a maximum level during the stationary phase. The amylase and protease were purified to homogeneity with molecular masses of 62 and 39 kDa, respectively. Optimal amylase activity was observed at 60°C, pH 10.0 and 12.5% NaCl. It was strongly stimulated by Ca²⁺, but inhibited by EDTA, DEPC and PAO, suggesting it was a metalloenzyme with histidine and cysteine residues located in its active site. Maltose was the main product of starch hydrolysis, indicating an b-amylase activity. The purified protease showed highest activity at 60°C, pH 9.0 and 10% NaCl. Complete inhibition by PMSF, DEPC, PAO and EDTA indicated it maybe a serine metalloprotease with histidine and cysteine residues essential for catalysis. Both enzymes were high active over broad temperature (40°C-80°C), NaCl concentration (0-20%) and pH (6.0-12.0) ranges, indicating their thermostable, halotolerant and alkali-stable nature. Also, they showed remarkable stability towards various surfactants. Results from the present study suggested the enzymes produced by Halobacillus sp. LY4 may have considerable potential for industrial application from the perspectives of their properties.