ReviewInternational journal of molecular sciences2015
Recombinant Lipases and Phospholipases and Their Use as Biocatalysts for Industrial Applications.
Review in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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Who cites it
72 citing papers in PubMed, 343 citations in OpenAlex.
- Lipases: An Overview.Methods in molecular biology (Clifton, N.J.) · 2027Review
- Lipase ITB 2.1: a structure- and function-validated model for anti-obesity drug screening.Molecular diversity · 2026Article
- Genetically engineered lipases: advances in expression and upscaling for industrial applications.Archives of microbiology · 2026Review
- Production of Novel Thermostable Esterases fromInternational journal of molecular sciences · 2026Article
- Extracellular Vesicles fromInternational journal of molecular sciences · 2025Article
- Advancements in Microbial Applications for Sustainable Food Production.Foods (Basel, Switzerland) · 2025Review
- Computational Modelling and Molecular Docking of Industrial Leather Enzymes.Molecular biotechnology · 2025Review
- Plants lipases: challenges, recent advances, and future prospects - a review.Bioprocess and biosystems engineering · 2025Review
- Genetically modified lipases as biocatalysts for diacylglycerol production in the food industry: a critical review.Archives of microbiology · 2025Review
- Characterization and molecular dynamics simulation of Lk2 lipase expressed in Pichia pastoris.Molecular biology reports · 2025Article
- Microbial lipases: advances in production, purification, biochemical characterization, and multifaceted applications in industry and medicine.Microbial cell factories · 2025Review
- ImmobilizedFrontiers in bioengineering and biotechnology · 2025Article
- Use of genomics & proteomics in studying lipase producing microorganisms & its application.Food chemistry. Molecular sciences · 2024Article
- Genome-resolved analysis of Serratia marcescens strain SMTT infers niche specialization as a hydrocarbon-degrader.DNA research : an international journal for rapid publication of reports on genes and genomes · 2024Article
- Structural Insights into Cold-Active Lipase from Glaciozyma antarctica PI12: Alphafold2 Prediction and Molecular Dynamics Simulation.Journal of molecular evolution · 2024Article
- A Comprehensive Transcriptomic and Proteomics Analysis of Candidate Secretory Proteins in Rose Grain Aphid,Current issues in molecular biology · 2024Article
- Functionally overlapping intra- and extralysosomal pathways promote bis(monoacylglycero)phosphate synthesis in mammalian cells.Nature communications · 2024Article
- Cold-Active Lipase from the Ice CaveMolecules (Basel, Switzerland) · 2024Article
- De novo transcriptome assembly and differential gene expression analysis in different developmental stages of Agriotes sputator (click beetle).Scientific reports · 2024Article
- Comprehensive Insights into Microbial Lipases: Unveiling Structural Dynamics, Catalytic Mechanism, and Versatile Applications.Current microbiology · 2024Review
12 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipases and phospholipases are interfacial enzymes that hydrolyze hydrophobic ester linkages of triacylglycerols and phospholipids, respectively. In addition to their role as esterases, these enzymes catalyze a plethora of other reactions; indeed, lipases also catalyze esterification, transesterification and interesterification reactions, and phospholipases also show acyltransferase, transacylase and transphosphatidylation activities. Thus, lipases and phospholipases represent versatile biocatalysts that are widely used in various industrial applications, such as for biodiesels, food, nutraceuticals, oil degumming and detergents; minor applications also include bioremediation, agriculture, cosmetics, leather and paper industries. These enzymes are ubiquitous in most living organisms, across animals, plants, yeasts, fungi and bacteria. For their greater availability and their ease of production, microbial lipases and phospholipases are preferred to those derived from animals and plants. Nevertheless, traditional purification strategies from microbe cultures have a number of disadvantages, which include non-reproducibility and low yields. Moreover, native microbial enzymes are not always suitable for biocatalytic processes. The development of molecular techniques for the production of recombinant heterologous proteins in a host system has overcome these constraints, as this allows high-level protein expression and production of new redesigned enzymes with improved catalytic properties. These can meet the requirements of specific industrial process better than the native enzymes. The purpose of this review is to give an overview of the structural and functional features of lipases and phospholipases, to describe the recent advances in optimization of the production of recombinant lipases and phospholipases, and to summarize the information available relating to their major applications in industrial processes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.