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Research Progress on the Processing and Modification of Lipid Compounds in Food

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Food Chemistry".

Deadline for manuscript submissions: 31 December 2024 | Viewed by 541

Special Issue Editor

JNU-UPM International Joint Laboratory on Plant Oil Processing and Safety, Department of Food Science and Engineering, Jinan University, Guangzhou 510632, China
Interests: processing and modification of lipids

Special Issue Information

Dear Colleagues,

In the contemporary food industry, the focus on health, nutrition, and sustainability has escalated the exploration and modification of lipid compounds. Lipids play a vital role in food formulation, sensory properties, and overall nutritional value. As consumer 

preferences evolve towards healthier and more sustainable options, the processing and modification of lipid compounds have become crucial areas of research and development.

Enhancing lipid stability, reducing unhealthy trans fats, and incorporating beneficial fatty acids are among the pivotal research directions in this domain. While considerable progress has been made in understanding lipid chemistry and functionality, there remains a pressing need for innovative processing methods and modifications that can improve the nutritional profile and sensory attributes of food products.

This Special Issue aims to provide a forum for researchers to present current and recent developments in the processing and modification of lipid compounds in food. We welcome original research papers and review articles addressing various aspects of lipid processing, modification, and application in food.

Dr. Zhen Zhang
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.

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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

  • lipid crystallization
  • lipid oxidation
  • enzymatic lipid modification
  • processing
  • health benefits
  • nutritional lipids
  • synthesis

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Published Papers (1 paper)

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Research

16 pages, 5535 KiB  
Article
Immobilization of Lipase from Thermomyces Lanuginosus and Its Glycerolysis Ability in Diacylglycerol Preparation
by Rui Xie, Yee-Ying Lee, Pengkai Xie, Chin-Ping Tan, Yong Wang and Zhen Zhang
Molecules 2024, 29(17), 4141; https://doi.org/10.3390/molecules29174141 - 31 Aug 2024
Viewed by 418
Abstract
In the glycerolysis process for diacylglycerol (DAG) preparation, free lipases suffer from poor stability and the inability to be reused. To address this, a cost-effective immobilized lipase preparation was developed by cross-linking macroporous resin with poly (ethylene glycol) diglycidyl ether (PEGDGE) followed by [...] Read more.
In the glycerolysis process for diacylglycerol (DAG) preparation, free lipases suffer from poor stability and the inability to be reused. To address this, a cost-effective immobilized lipase preparation was developed by cross-linking macroporous resin with poly (ethylene glycol) diglycidyl ether (PEGDGE) followed by lipase adsorption. The selected immobilization conditions were identified as pH 7.0, 35 °C, cross-linking agent concentration 2.0%, cross-linking time 4 h, lipase amount 5 mg/g of support, and adsorption time 4 h. Enzymatic properties of the immobilized lipase were analyzed, revealing enhanced pH stability, thermal stability, storage stability, and operational stability post-immobilization. The conditions for immobilized enzyme-catalyzed glycerolysis to produce DAG were selected, demonstrating the broad applicability of the immobilized lipase. The immobilized lipase catalyzed glycerolysis reactions using various oils as substrates, with DAG content in the products ranging between 35 and 45%, demonstrating broad applicability. Additionally, the changes during the repeated use of the immobilized lipase were characterized, showing that mechanical damage, lipase leakage, and alterations in the secondary structure of the lipase protein contributed to the decline in catalytic activity over time. These findings provide valuable insights for the industrial application of lipase. Full article
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