Surfactant-free beamhouse technology of leather manufacturing: Removing constraints for the breakdown of natural fats catalyzed by lipase

Li, Shan; Luo, Fengxiang; Chattha, Sadaqat Ali; Zhang, Chunxiao; Peng, Biyu; Mu, Changdao

doi:10.1016/j.jclepro.2020.121187

Cited by 5 publications

(1 citation statement)

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“…These enzymes, classified as triacylglycerol 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 areas, including the leather industry (Abol Fotouh et al 2016;Li et al 2020), food products segment (Hassan et al 2019;Akil et al 2020) and also in the energy sector (Hassan et al 2019). Microorganisms of the genus Aspergillus, Calvatia, Rhizopus, Rhodotorula and Yarrowia can produce constitutive lipase (gene expression) that can be partially induced with the aid of triacylglycerols or fatty acids.…”

Section: Introductionmentioning

confidence: 99%

Catalytic and physical features of a naturally immobilized Yarrowia lipolytica lipase in cell debris (LipImDebri) displaying high thermostability

et al. 2020

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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 (R 2 = 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.

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