Catalytic and physical features of a naturally immobilized Yarrowia lipolytica lipase in cell debris (LipImDebri) displa
- PDF / 1,337,824 Bytes
- 12 Pages / 595.276 x 790.866 pts Page_size
- 63 Downloads / 202 Views
ORIGINAL ARTICLE
Catalytic and physical features of a naturally immobilized Yarrowia lipolytica lipase in cell debris (LipImDebri) displaying high thermostability Jully Lacerda Fraga1 · Adrian Chaves Beserra da Penha1 · Emília Akil2 · Kelly Alencar Silva3 · Priscilla Filomena Fonseca Amaral1 Received: 3 August 2020 / Accepted: 15 September 2020 © King Abdulaziz City for Science and Technology 2020
Abstract 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 (kd = 0.246 h−1; t1/2 = 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. Keywords Cell-bounded enzymes · Cell debris · Yarrowia lipolytica · Thermostability · Electron microscopy · Lipase
Introduction Lipases from microbial source have been preferred for industrial production and by scientific community when compared to enzymes produced by plants or animals (Treichel et al. 2010). These enzymes, classified as triacylglycerol * Priscilla Filomena Fonseca Amaral [email protected] 1
Departamento de Eng. Bioquímica, Escola de Química, Centro de Tecnologia, Universidade Federal do Rio de Janeiro, Cidade Universitária, Avenida Athos da Silveira Ramos, N° 123, Bloco E, Rio de Janeiro, RJ CEP 21941‑900, Brazil
2
Laboratório de Bioquímica Nutricional e de Alimentos, Instituto de Química, Centro de Tecnologia, Universidade Federal do Rio de Janeiro, Cidade Universitária, Avenida Athos da Silveira Ramos, N° 149, Bloco A, sala 528A, Rio de Janeiro, RJ CEP 21941‑909, Brazil
3
Centro de Ciências Médicas, Faculdade de Farmácia, Departamento de Bromatologia, Universidade Federal Fluminense, Niterói, RJ 24241‑002, Brazil
acylhydrolases (EC 3.1.1.3), can hydrolyze and synthetize ester bounds, catalyzing esterification, interesterification, and transesterification reactions (Luković et al. 2011; Gupta et al. 2015). In this sense, lipases find new applications in several industrial area
Data Loading...
