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Journals
Biomolecules
Special Issues
Advances in Lipases and Lipases Modification
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Advances in Lipases and Lipases Modification

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Lipids".

Deadline for manuscript submissions: closed (31 December 2023) | Viewed by 10393

Special Issue Editor

Prof. Dr. Yunjun Yan

E-Mail Website
Guest Editor
School of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, China
Interests: nanocomposite; bio-based materials; synthesis; modification; characterization
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Lipases have remarkable properties and broad application prospects in a variety of industries, such as food, chemistry, energy, agriculture, pharmaceuticals, etc. In recent years, scientists have achieved extraordinary achievements and made significant progress in the field of lipase research. Many lipases have been excavated, characterized, engineered and even created through protein engineering, and numerous genetic engineering strategies have been developed for efficient heterologous expression of lipases. Despite this, performance and activity are still important factors limiting the large-scale application of lipases. Therefore, this Special Issue welcomes comprehensive reviews or original research papers focusing on the following topics, among other relevant areas: screening and retrieval of novel lipases with excellent characteristics, lipase modification, regulation mechanism for lipase expression, high-efficiency expression of lipases and innovative industrial application of lipases. We look forward to receiving your contributions.

Prof. Dr. Yunjun Yan
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Biomolecules is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • lipases
  • modification
  • expression
  • application

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Published Papers (2 papers)

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Research

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11 pages, 982 KiB  
Article
Single-Particle Tracking of Thermomyces lanuginosus Lipase Reveals How Mutations in the Lid Region Remodel Its Diffusion
by Josephine F. Iversen, Søren S.-R. Bohr, Henrik D. Pinholt, Matias E. Moses, Lars Iversen, Sune M. Christensen, Nikos S. Hatzakis and Min Zhang
Biomolecules 2023, 13(4), 631; https://doi.org/10.3390/biom13040631 - 31 Mar 2023
Cited by 8 | Viewed by 2818
Abstract
The function of most lipases is controlled by the lid, which undergoes conformational changes at a water–lipid interface to expose the active site, thus activating catalysis. Understanding how lid mutations affect lipases’ function is important for designing improved variants. Lipases’ function has been [...] Read more.
The function of most lipases is controlled by the lid, which undergoes conformational changes at a water–lipid interface to expose the active site, thus activating catalysis. Understanding how lid mutations affect lipases’ function is important for designing improved variants. Lipases’ function has been found to correlate with their diffusion on the substrate surface. Here, we used single-particle tracking (SPT), a powerful tool for deciphering enzymes’ diffusional behavior, to study Thermomyces lanuginosus lipase (TLL) variants with different lid structures in a laundry-like application condition. Thousands of parallelized recorded trajectories and hidden Markov modeling (HMM) analysis allowed us to extract three interconverting diffusional states and quantify their abundance, microscopic transition rates, and the energy barriers for sampling them. Combining those findings with ensemble measurements, we determined that the overall activity variation in the application condition is dependent on surface binding and lipase mobility when bound. Specifically, the L4 variant with a TLL-like lid and wild-type (WT) TLL displayed similar ensemble activity, but WT bound stronger to the surface than L4, while L4 had a higher diffusion coefficient and thus activity when bound to the surface. These mechanistic elements can only be de-convoluted by our combined assays. Our findings offer fresh perspectives on the development of the next iteration of enzyme-based detergent. Full article
(This article belongs to the Special Issue Advances in Lipases and Lipases Modification)
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Review

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16 pages, 1439 KiB  
Review
Activation Mechanisms and Diverse Functions of Mammalian Phospholipase C
by Kaori Kanemaru and Yoshikazu Nakamura
Biomolecules 2023, 13(6), 915; https://doi.org/10.3390/biom13060915 - 31 May 2023
Cited by 18 | Viewed by 6904
Abstract
Phospholipase C (PLC) plays pivotal roles in regulating various cellular functions by metabolizing phosphatidylinositol 4,5-bisphosphate in the plasma membrane. This process generates two second messengers, inositol 1,4,5-trisphosphate and diacylglycerol, which respectively regulate the intracellular Ca2+ levels and protein kinase C activation. In [...] Read more.
Phospholipase C (PLC) plays pivotal roles in regulating various cellular functions by metabolizing phosphatidylinositol 4,5-bisphosphate in the plasma membrane. This process generates two second messengers, inositol 1,4,5-trisphosphate and diacylglycerol, which respectively regulate the intracellular Ca2+ levels and protein kinase C activation. In mammals, six classes of typical PLC have been identified and classified based on their structure and activation mechanisms. They all share X and Y domains, which are responsible for enzymatic activity, as well as subtype-specific domains. Furthermore, in addition to typical PLC, atypical PLC with unique structures solely harboring an X domain has been recently discovered. Collectively, seven classes and 16 isozymes of mammalian PLC are known to date. Dysregulation of PLC activity has been implicated in several pathophysiological conditions, including cancer, cardiovascular diseases, and neurological disorders. Therefore, identification of new drug targets that can selectively modulate PLC activity is important. The present review focuses on the structures, activation mechanisms, and physiological functions of mammalian PLC. Full article
(This article belongs to the Special Issue Advances in Lipases and Lipases Modification)
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