Unveiling the applications of membrane proteins from oil bodies: leading the way in artificial oil body technology and other biotechnological advancements

Abstract

Oil bodies (OBs) function as organelles that store lipids in plant seeds. An oil body (OB) is encased by a membrane composed of proteins (e.g., oleosins, caleosins, and steroleosins) and a phospholipid monolayer. The distinctive protein-phospholipid membrane architecture of OBs imparts exceptional stability even in extreme environments, thereby sparking increasing interest in their structure and properties. However, a comprehensive understanding of the structure-activity relationships determining the stability and properties of oil bodies requires a more profound exploration of the associated membrane proteins, an aspect that remains relatively unexplored. In this review, we aim to summarize and discuss the structural attributes, biological functions, and properties of OB membrane proteins. From a commercial perspective, an in-depth understanding of the structural and functional properties of OBs is important for the expansion of their applications by producing artificial oil bodies (AOB). Besides exploring their structural intricacies, we describe various methods that are used for purifying and isolating OB membrane proteins. These insights may provide a foundational framework for the practical utilization of OB membrane proteins in diverse applications within the realm of AOB technology, including biological and probiotic delivery, protein purification, enzyme immobilization, astringency detection, and antibody production.

Graphical Abstract

Keywords:

• Oil bodies
• membrane protein
• artificial oil body
• stability
• biological delivery

Authors’ contributions

Yi Liao developed the ideas of the manuscript and drafted and edited manuscript. Zhenxiao Wang edited the figures. Yukun Pei edited the tables and revised the references. Shizhang Yan provided suggestions and discussions on the technical part. Tianyao Chen corrected the manuscript. Baokun Qi and Yang Li revised the final manuscript.

Disclosure statement

The authors confirm that they have no conflicts of interest with respect to the work described in this manuscript.

Additional information

Funding

The National Natural Science Foundation of China (No. 32172141).