Lipases (triacylglycerol hydrolases E.C. 3.1.1.3) are enzymes produced by mammals, plants, fungi and bacteria that catalyze the hydrolysis of triacylglycerols into glycerol and fatty acids. Lipases...

Lipases: From Production to Applications

Aromatics and their derivatives are valuable chemicals with a plethora of important applications and thus play an integral role in modern society. Their current production relies mostly on the exploitation of petroleum resources. Independency from dwindling fossil resources and rising environmental concerns are major driving forces for the transition towards the production of sustainable aromatics from renewable feedstocks or waste streams. Whole-cell biocatalysis is a promising strategy that allows the valorization of highly abundant, low-cost substrates. In the last decades, extensive efforts are undertaken to allow the production of a wide spectrum of different aromatics and derivatives using microbes as biocatalysts. Pseudomonads are intriguing hosts for biocatalysis, as they display unique characteristics beneficial for the production of aromatics, including a distinct tolerance and versatile metabolism. This review highlights biotechnological applications of Pseudomonas as host for the production of aromatics and derived compounds. This includes their de novo biosynthesis from renewable resources, biotransformations in single- and biphasic fermentation setups, metabolic funneling of lignin-derived aromatics, and the upcycling of aromatic monomers from plastic waste streams. Additionally, this review provides insights into unique features of Pseudomonads that make them exceptional hosts for aromatics biotechnology and discusses engineering strategies.

https://onlinelibrary.wiley.com/doi/pdf/10.1002/biot.201900569

Pseudomonas as Versatile Aromatics Cell Factory.

An effective method for reducing free fatty acid content of high-acid rice bran oil by enzymatic amidation

Determination and health risk assessment of heavy metals in imported rice bran oil in Iran

The advancements in biotechnology over time have led to an increase in the demand of pure, soluble and functionally active proteins. Recombinant protein production has thus been employed to obtain high expression of purified proteins in bulk. E. coli is considered as the most desirable host for recombinant protein production due to its inexpensive and fast cultivation, simple nutritional requirements and known genetics. Despite all these benefits, recombinant protein production often comes with drawbacks, such as, the most common being the formation of inclusion bodies due to improper protein folding. Consequently, this can lead to the loss of the structure-function relationship of a protein. Apart from various strategies, one major strategy to resolve this issue is the use of molecular chaperones that act as folding modulators for proteins. Molecular chaperones assist newly synthesized, aggregated or misfolded proteins to fold into their native conformations. Chaperones have been widely used to improve the expression of various proteins which are otherwise difficult to produce in E. coli. Here, we discuss the structure, function, and role of major E. coli molecular chaperones in recombinant technology such as trigger factor, GroEL, DnaK and ClpB.

A Review: Molecular Chaperone-mediated Folding, Unfolding and Disaggregation of Expressed Recombinant Proteins

The ability of immobilized lipase from Rhizomucor miehei (Lipozyme RM IM) to catalyze the reaction of high-acid rice bran oil (RBO) and monoglyceride (MG) for diacylglycerol-enriched rice bran oil (RBO-DG) preparation was investigated. The effects of substrate ratio, reaction temperature, time, and enzyme load on the respective content of free fatty acid (FFA) and DG in the final RBO-DG products was investigated. Enzyme screening on the reaction was also investigated. Response surface methodology (RSM) was used to optimize the effects of the reaction temperature (50–70 °C), the enzyme load (2–6 %; relative to the weight of total substrates), and the reaction time (4–8 h) on the respective content of FFA and DG. Validation of the RSM model was verified by the good agreement between the experimental and the predicted values. The optimum preparation conditions were as follows: MG/RBO, 0.25; temperature, 56 °C; enzyme load, 4.77 %; and reaction time, 5.75 h. Under the suggested conditions, the respective content of FFA and DG was 0.28 and 27.98 %, respectively. Repeated reaction tests indicated that Lipozyme RM IM could be used nine times under the optimum conditions with 90 % of its original catalytic activity still retained.

Lipase-Catalyzed Preparation of Diacylglycerol-Enriched Oil from High-Acid Rice Bran Oil in Solvent-Free System

An active D-hydantoinase from Pseudomonas fluorescens was heterogeneously overexpressed in Escherichia coli BL21(DE3) and designated as D-PfHYD. Sequence and consensus analysis suggests that D-PfHYD belongs to the dihydropyrimidinase/hydantoinase family and possesses catalytic residues for metal ion and hydantoin binding. D-PfHYD was purified to homogeneity by nickel affinity chromatography for characterization. D-PfHYD is a homotetramer with molecular weight of 215 kDa and specific activity of 20.9 U mg(-1). D-PfHYD showed the highest activity at pH 9.0 and 60 °C. Metal ions such as Mn(2+), Fe(2+), and Fe(3+) could activate D-PfHYD with 20 % improvement. Substrate specificity analysis revealed that purified D-PfHYD preferred aliphatic to aromatic 5'-monosubstituted hydantoins. Among various strategies tested, chaperone GroES-GroEL was efficient in improving the soluble expression of D-PfHYD. Employing 1.0 g L(-1) recombinant E. coli BL21(DE3)-pET28-hyd/pGRO7 dry cells, 100 mM isobutyl hydantoin was converted into D-isoleucine with 98.7 % enantiomeric excess (ee), isolation yield of 78.3 %, and substrate to biocatalyst ratio of 15.6. Our results suggest that recombinant D-PfHYD could be potentially applied in the synthesis of D-amino acids.

Characterization and Soluble Expression of D-Hydantoinase from Pseudomonas fluorescens for the Synthesis of D-Amino Acids.

The invention relates to a preparation method of rice bran oil rich in diacylglycerol, belonging to the fields of the deep processing and the modification of grease. In the invention, oleic acid glycerol ester and rice bran oil with a high acid value are used as raw materials, influence factors, such as reaction temperature, reaction time, lipase addition, and the like are optimized under vacuum and rotating conditions by adopting a reaction for catalyzing and preparing lipase lipozyme RM IM and the optimal process conditions and parameters for preparing the rice bran oil rich in the diacylglycerol are confirmed. The invention takes favorable guiding action on the development of a novel process for the deep processing of the rice bran oil and lays the foundation for establishing a processing process of healthy and nutritious rice bran oil.

Preparation method of rice bran oil rich in diacylglycerol

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Lipase-Catalyzed Preparation of Diacylglycerol-Enriched Oil from High-Acid Rice Bran Oil in Solvent-Free System

Characterization and Soluble Expression of D-Hydantoinase from Pseudomonas fluorescens for the Synthesis of D-Amino Acids.

Preparation method of rice bran oil rich in diacylglycerol