Rhizopus oryzae Lipase, a Promising Industrial Enzyme: Biochemical Characteristics, Production and Biocatalytic Applications

Abstract

Lipases are biocatalysts with a significant potential to enable a shift from current pollutant manufacturing processes to environmentally sustainable approaches. The main reason of this prospect is their catalytic versatility as they carry out several industrially relevant reactions as hydrolysis of fats in water/lipid interface and synthesis reactions in solvent-free or non-aqueous media such as transesterification, interesterification and esterification. Because of the outstanding traits of Rhizopus oryzae lipase (ROL), 1,3-specificity, high enantioselectivity and stability in organic media, its application in energy, food and pharmaceutical industrial sector has been widely studied. Significant advances have been made in the biochemical characterisation of ROL particularly in how its activity and stability are affected by the presence of its prosequence. In addition, native and heterologous production of ROL, the latter in cell factories like Escherichia coli, Saccharomyces cerevisiae and Komagataella phaffii (Pichia pastoris), have been thoroughly described. Therefore, in this review, we summarise the current knowledge about R. oryzae lipase (i) biochemical characteristics, (ii) production strategies and (iii) potential industrial applications.

Development of a green integrated process for biodiesel esters production: Use of fermented macaúba cake as biocatalyst for macaúba acid oil transesterification

“…R. oryzae lipase is a 1,3‐specific lipase and the maximum conversion achieved (about 70%) is close to the theoretical maximum percentage (66%), without considering acyl migration from the sn‐2 position to the sn‐1 or sn‐3 positions, as described by López‐Fernández et al (2020). On the other hand, R. miehei lipase is also 1–3 positional specific lipase and as it was suggested in R. miehei results, different lipase pools were presented in the DFS.…”

Rhizopus oryzae-Mediated Green Synthesis of Magnesium Oxide Nanoparticles (MgO-NPs): A Promising Tool for Antimicrobial, Mosquitocidal Action, and Tanning Effluent Treatment

“…Rhizopus oryaze are characterized by their platform’s highly secondary metabolites such as chemicals (fumaric acid, lactic acid, and ethanol), enzymes, fermentative compounds, and a wide range of by-products [ 44 , 45 ]. This wide range of metabolites increases the possibilities of R. oryaze to incorporate into various biomedical and biotechnological applications.…”

Constitutive Expression in Komagataella phaffii of Mature Rhizopus oryzae Lipase Jointly with Its Truncated Prosequence Improves Production and the Biocatalyst Operational Stability

“…However, even if the soluble and active production of lipases was achieved, the fact that the enzymes were intracellularly produced-therefore requiring further purification steps-as well as the lack of protein processing mechanisms, since the lipase that contained the complete prosequence was not properly hydrolyzed, promoted the assessment of the yeasts S. cerevisiae and K. phaffii as potential sources for this enzyme. The different proteolytic processing imposed by Kex2-like protease in S. cerevisiae enabled the production of two lipase forms by the gene encoding the whole prosequence linked to the mature sequence (w-proROLgene), unlike observed with E. coli; however, no activity was detected when only the mature sequence gene (rROL-gene) was expressed, which highlights the importance of the prosequence for efficient production of the lipase [5]. With the methylotrophic yeast K. phaffii, only the cleaved form of ROL was obtained after w-proROL-gene expression, which underlies the increased activity of Kex2-like protease in this microorganism [23].…”

“…3.1.1.3), which are the most widely used biocatalysts after proteases and amylases, catalyze a wide range of industrially interesting reactions including esterification, transesterification and interesterification [3,4]. Specifically, Rhizopus oryzae lipase (ROL) has been the subject of much study on account of a number of favorable traits such as 1,3-regioespecificity, high thermostability, tolerance of organic solvents, and the ability to produce flavors, biodiesel and structured lipids [5]. All lipases from the genus Rhizopus are synthesized as precursor forms sharing a common structure.…”

“…ROL can be effectively immobilized in these three ways (e.g., by adsorption [16], covalent binding [17], entrapment into alginate beads [18] or formation of cross-linked aggregates [19]). Immobilized biocatalysts have proved highly suitable for industrial-scale applications such as biodiesel and flavor production [5].…”