Related Experiment Video
Updated: Oct 23, 2025
06:16
Preparation Of Gushukang GSK Granules for In Vivo and In Vitro Experiments
Published on: May 9, 2019
7.8K
Ginkgo Seed Proteins: Characteristics, Functional Properties and Bioactivities
Wanning Liu1,2, Minmin Zou1,2, Yaosong Wang1,2
1Co-Innovation Center for the Sustainable Forestry in Southern China, Nanjing Forestry University, Nanjing, 210037, China.
Plant Foods for Human Nutrition (Dordrecht, Netherlands)
|August 24, 2021
Summary
Ginkgo seed proteins (GSPs) offer excellent functional properties and bioactivities, making them a valuable ingredient for food applications. Their easy separation and rich nutritional profile highlight their potential.
Area of Science:
- Plant Biochemistry
- Food Science
- Nutritional Science
Background:
- Ginkgo biloba L., a
- living fossil
- plant, is widely cultivated in China and recognized for its medicinal and health benefits.
Purpose of the Study:
- This review summarizes the separation methods, physicochemical characteristics, functional properties, and bioactivities of Ginkgo seed proteins (GSPs).
- It also explores potential food applications and future prospects of GSPs.
Main Methods:
- Literature review of studies on Ginkgo seed protein separation, characterization, bioactivities, and applications.
- Comparative analysis of GSP properties with other seed proteins.
Main Results:
- Ginkgo seed proteins (GSPs) exhibit favorable functional properties and contain no restricted amino acids, facilitating their use as food ingredients.
- Purified GSP isolates demonstrate significant antimicrobial and antioxidative activities, indicating their bioactive potential.
Conclusions:
- Ginkgo seed proteins (GSPs) possess valuable characteristics for food ingredient applications.
- Further research into their bioactivities and food applications is warranted.
More Related Videos
Related Concept Videos
01:21Matrix Proteoglycans and Glycoproteins
4.3K
Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...
4.3K
01:25Protein Glycosylation
7.9K
Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
Glycosylation occurs in...
7.9K
01:22Activation and Inactivation of G Proteins
8.0K
Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high...
8.0K