Short-chain aliphatic esters possess pleasant fruity and fatty aromas and are widely used in food products and cosmetics. Cutinases can catalyze the synthesis of short-chain aliphatic esters from organic acids and alcohols. Compared with chemical synthesis, enzymatic synthesis of short-chain aliphatic esters has advantages such as mild reaction conditions and environmental friendliness. The present study aimed to identify novel cutinases and investigate their application potential in the efficient synthesis of short-chain aliphatic esters. A cutinase gene (UtCut) was cloned from Umezawaea tangerine and expressed in Escherichia coli BL21 (DE3). The recombinant enzyme (UtCut) was purified by affinity chromatography and characterized, and its effects on the synthesis of short-chain aliphatic esters were determined. The results indicated that UtCut shared the highest similarity of 74.9% with the cutinase derived from Amycolatopsis mediterranei. The specific activity of UtCut was 279.29 U•mg-1, and its optimum pH and temperature were 8.0 and 35 ℃, respectively. The enzyme maintained its stability at temperatures up to 35 ℃ and within the pH range of 6.0~8.5. It showed the highest hydrolytic activity toward pNPH (C6) and tributyrin. At an enzyme concentration of 25 U•mL-1 and temperature of 35 ℃, an esterification rate of 100% was obtained for the synthesis of ethyl caproate. The newly identified cutinase may have application potential in the flavor ester production industry.