Lipases are the industrially important biocatalysts, which are envisioned to have tremendous applications in the manufacture of a wide range of products. Their unique properties such as better stability, selectivity and substrate specificity position them as the most expansively used industrial enzymes. The research on production and applications of lipases is ever growing and there exists a need to have a latest review on the research findings of lipases. The present review aims at giving the latest and broadest overall picture of research and development on lipases by including the current studies and progressions not only in the diverse industrial application fields of lipases, but also with regard to its structure, classification and sources. Also, a special emphasis has been made on the aspects such as process optimization, modeling, and design that are very critical for further scale-up and industrial implementation. The detailed tabulations provided in each section, which are prepared by the exhaustive review of current literature covering the various aspects of lipase including its production and applications along with example case studies, will serve as the comprehensive source of current advancements in lipase research. This review will be very useful for the researchers from both industry as well as academia in promoting lipolysis as the most promising approaches to intensified, greener and sustainable processes. © 2017 American Institute of Chemical Engineers Biotechnol. Prog., 34:5-28, 2018.

Recent advances on sources and industrial applications of lipases

Biosurfactants are economically most sought after biotechnological compounds of the 21st century. However, inefficient bioprocessing has mitigated the economical commercial production of these compounds. Although much work is being done on the use of low-cost substrates for their production, a paucity of literature exists on the upcoming bioprocess optimization strategies and their successes and potential for economical biosurfactant production. This review discusses some of the latest developments and most promising strategies to enhance and economize the biosurfactant production process. Recent market analysis, developments in the field of optimally formulated cost credit substrates for enhanced product formation and subsequent process economization are few of the critical aspects highlighted here. Use of nanoparticles and coproduction of biosurfactant along with other commercially important compounds like enzymes, are other upcoming bioprocess intensification strategies. The recent developments discussed here would not only give an overview of pertinent parameters for economic biosurfactant production but would also bring to fore multiple strategies that would open up new avenues of research on biosurfactant production. This would go a long way in making biosurfactants a commercially successful compound of the current century.

https://sfamjournals.onlinelibrary.wiley.com/doi/pdf/10.1111/jam.14057

Biosurfactant production: emerging trends and promising strategies.

Lipase (E.C.3.1.1.3) belongs to the hydrolases and is also known as fat splitting, glycerol ester hydrolase or triacylglycerol acylhydrolase. Lipase catalyzes the hydrolysis of triglycerides converting them to glycerol and fatty acids in an oil-water interface. These are widely used in food, dairy, flavor, pharmaceuticals, biofuels, leather, cosmetics, detergent, and chemical industries. Lipases are of plant, animal, and microbial origin, but microbial lipases are produced at industrial level and represent the most widely used class of enzymes in biotechnological applications and organic chemistry. Phylogenetic analysis and comparison of residues around GxSxG motif provided an insight to the diversity among bacterial lipases. A variety of para-Nitrophenyl (p-NP) esters having C2 to C16 (p-NP acetate to p-NP palmitate) in their fatty acid side chain can be hydrolyzed by bacterial lipases. Large heterogeneity has been observed in molecular and catalytic characteristics of lipases including molecular mass; 19–96 kDa, Km; 0.0064–16.58 mM, Kcat; 0.1665–1.0 × 104 s−1 and Kcat/Km; 26.02–7377 s-1/mM. Optimal conditions of their working temperature and pH have been stated 15–70 °C and 5.0–10.8, respectively and are strongly associated with the type and growth conditions of bacteria. Surface hydrophobicity, enzyme activity, stability in organic solvents and at high temperature, proteolytic resistance and substrate tolerance are the properties of bacterial lipases that have been improved by engineering. Bacterial lipases have been extensively studied during last decade. However, their wider applications demand a detailed review on purification, catalytic characterization and applications of lipases.

Bacterial lipases: A review on purification and characterization.

Plastic pollution is a growing environmental problem, in part due to the extremely stable and durable nature of this polymer. As recycling does not provide a complete solution, research has been focusing on alternative ways of degrading plastic. Fungi provide a wide array of enzymes specialized in the degradation of recalcitrant substances and are very promising candidates in the field of plastic degradation. This review examines the present literature for different fungal enzymes involved in plastic degradation, describing their characteristics, efficacy and biotechnological applications. Fungal laccases and peroxidases, generally used by fungi to degrade lignin, show good results in degrading polyethylene (PE) and polyvinyl chloride (PVC), while esterases such as cutinases and lipases were successfully used to degrade polyethylene terephthalate (PET) and polyurethane (PUR). Good results were also obtained on PUR by fungal proteases and ureases. All these enzymes were isolated from many different fungi, from both Basidiomycetes and Ascomycetes, and have shown remarkable efficiency in plastic biodegradation under laboratory conditions. Therefore, future research should focus on the interactions between the genes, proteins, metabolites and environmental conditions involved in the processes. Further steps such as the improvement in catalytic efficiency and genetic engineering could lead these enzymes to become biotechnological applications in the field of plastic degradation.

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Fungal Enzymes Involved in Plastics Biodegradation

– Filamentous fungi can easily degrade agro-industrial wastes in solid-state fermentation processes, synthesizing many important commercial biocompounds, such as lipolytic enzymes. The aim of this study was to evaluate the effect of the composition of the solid culture medium on the production of lipolytic enzymes by the fungus Aspergillus niger. Rice, wheat and soybean bran were mixed to prepare the culture medium, which was supplemented with glucose, glycerol or soybean oil. Four mixture experimental designs were used to find the best medium for enzyme production. According to our results, the highest lipolytic activity values were achieved with a mixture of rice bran and glycerol (19.844 U·g -1 ) or with rice bran only (13.267 U·g). Thus, the lipolytic enzyme could be produced without any additional carbon source apart from rice bran, although glycerol addition induced a higher production. Keywords : Enzyme; Fungus; Agro-industrial wastes; Carbon source. INTRODUCTION Lipases (triacylglycerol acyl hydrolases, EC 3.1.1.3) are enzymes that catalyze the hydrolysis and the synthesis of esters (Qamsari et al., 2011). Some lipases are capable of catalyzing the esterification, transesterification and interesterification of lipids (Burkert et al., 2004; Colla et al., 2010; Martins et al., 2008), water activity (a

/pdf/lipase-production-by-aspergillus-niger-grown-in-different-22e5zjd1rp.pdf

LIPASE PRODUCTION BY Aspergillus niger GROWN IN DIFFERENT AGRO-INDUSTRIAL WASTES BY SOLID-STATE FERMENTATION

Lipases are one of the most promising enzymes in the chemical and biopharmaceutical industries. Numerous applications have been reported including fine chemistry, detergents formulation and biodiesel synthesis. Lipases are commonly produced by a wide variety of yeasts and filamentous fungi in submerged fermentation or solid-state fermentation. Filamentous fungi and yeasts usually behave more efficiently in solid-state fermentation and show greater productivities when compared to submerged fermentation. Although filamentous fungi adequately growth in solid-state fermentation, there are some limitations for cultivating them by this process. Here, a review is made about lipase production in solid-state fermentation. This includes the analysis of solid-state fermentation as a promising technology, characterization of growth media and ambient factors such as moisture, pH and temperature.

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Jesus Cordova

Papers

Fungal Lipase Production by Solid-State Fermentation