Lipase activity (337 U/g dry weight of cell debris) was detected in cell debris after ultrasound treatment of Yarrowia lipolytica cells cultivated in residual frying palm oil. It is a naturally immobilized lipase with protein content of 47%, herein called LipImDebri. This immobilized biocatalyst presents low hydrophobicity (8%), that can be increased adjusting pH and buffer type. Despite apparent intact cells, electron microscopy showed a shapeless and flat surface for LipImDebri and optical microscopy revealed no cell viability. Besides, an inferior mean diameter (3.4 mm) in relation to whole cells reveals structure modification. A high negative zeta potential value (− 33.86 mV) for pH 6 and 25 °C suggests that LipImDebri is a stable suspension in aqueous solution. Fourier Transform Infrared Spectra (FTIR) expose differences between LipImDebri and extracellular lipase extract signaling a physical interaction between enzyme and cell debris, which is possibly the reason for the high thermostability (k_d = 0.246 h⁻¹; t_1/2 = 2.82 h at 50 °C, pH 7.0). A good adjustment of LipImDebri kinetic data with Hill equation (R² = 0.95) exposes an allosteric behavior related to the presence of more than one lipase isoform. These features reveal that LipImDebri can be a good catalyst for industrial applications.

超声处理解脂耶氏酵母后，在细胞碎片中检测到脂肪酶活性（337 U/g 细胞碎片干重）在残留的煎炸棕榈油中培养的细胞。它是一种天然固定化脂肪酶，蛋白质含量为 47%，本文称为 LipImDebri。这种固定化生物催化剂具有低疏水性 (8%)，可以增加调节 pH 值和缓冲液类型。尽管细胞明显完整，但电子显微镜显示 LipImDebri 的表面无形状且平坦，光学显微镜显示没有细胞活力。此外，与整个细胞相比，较低的平均直径 (3.4 mm) 显示结构改变。pH 6 和 25 °C 的高负 zeta 电位值 (- 33.86 mV) 表明 LipImDebri 在水溶液中是一种稳定的悬浮液。傅立叶变换红外光谱 (FTIR) 揭示了 LipImDebri 和细胞外脂肪酶提取物之间的差异，表明酶和细胞碎片之间的物理相互作用，k _d  = 0.246 h ^-1；t _1/2  = 2.82 小时，50 °C，pH 7.0）。使用 Hill 方程 ( R ²  = 0.95)对 LipImDebri 动力学数据进行良好调整，揭示了与存在一种以上脂肪酶同种型相关的变构行为。这些特征表明 LipImDebri 可以成为工业应用的良好催化剂。