A lipase from Sporisorium reilianum SRZ2 (SRL) with 73% amino acid sequence identity to Candida antarctica lipase B (CALB) was cloned and overexpressed in Pichia pastoris. The recombinant SRL showed a preference for short-chain p-nitrophenyl esters. It achieved maximum activity at pH 8.0 and 65°C for p-nitrophenyl hexanoate (C6) with K_m and k_cat/K_m values of 0.14 mmol·L⁻¹ and 1712 min⁻¹ · mmol · L⁻¹ at 30°C, respectively. SRL displayed excellent thermostability and pH stability, retaining more than 79% of its initial activity after incubation at 60°C for 72 h and 75% at pH 3 to 11 for 72 h. It also maintained most of its activity in the presence of inhibitors and detergents except sodium dodecyl sulfate, and it tolerated organic solvents. SRL was covalently immobilized and successfully used for ethyl hexanoate synthesis in cyclohexane or in a solvent-free system with a high conversion yield (> 95%). Furthermore, high conversion yield was also achieved for the synthesis of various short-chain flavor esters when high substrate concentrations of 2 mol · L⁻¹ were applied. This study indicated that a CALB-type lipase from S. reilianum SRZ2 showed great potential in organic ester synthesis.

克隆了与南极假丝酵母脂肪酶B（CALB）具有73％氨基酸序列同一性的来自球形孢子虫SRZ2（SRL）的脂肪酶，并在毕赤酵母中过表达。重组SRL显示出对短链对硝基苯酯的偏爱。它在pH 8.0和65°C时对己酸对硝基苯酯（C6）具有最大活性，K _m和k _cat / K _m值为0.14mmol·L ^-1和1712 min ^-1 ·mmol·L ^-1分别在30°C下 SRL表现出出色的热稳定性和pH稳定性，在60°C孵育72小时后保持其初始活性的79％，在pH 3到11孵育72小时后保留75％的初始活性。除十二烷基硫酸钠外，它在阻聚剂和去污剂存在下也能保持其大部分活性，并且它能耐受有机溶剂。SRL被共价固定并成功用于环己烷或无溶剂系统中的己酸乙酯合成，具有很高的转化率（> 95％）。此外，当施加2mol·L ^-1的高底物浓度时，合成各种短链风味酯也实现了高转化率。这项研究表明，来自re链霉菌的CALB型脂肪酶 SRZ2在有机酯合成中显示出巨大潜力。