Research progress of yeast mannoproteins

doi:10.12211/2096-8280.2024-050

Abstract

Abstract:

Yeast mannoprotein is a non-fibrous glycoprotein localized on the outermost layer of yeast cell walls. As a natural functional ingredient, its commercial application is limited and currently only used as a wine stabilizer. To advance the development and broader commercialization of mannoprotein, this paper briefly outlines its structural characteristics, including the peptide chain, core region, and outer chain composition. The peptide chain forms the backbone of mannoprotein, while the core and outer chains are composed of various carbohydrate portions, predominantly mannose residues. This unique structure contributes to the diverse biological activities of mannoprotein. The advantages and disadvantages of acid, alkali, enzyme, and physical methods for extracting yeast mannoprotein are discussed. Acids and bases are effective for extracting yeast mannoprotein, but may compromise its structural integrity, while enzymatic extraction is less destructive, preserving the structure but with a higher cost. A systematic review is conducted on the biological activities of yeast mannoprotein in improving intestinal health, stimulating immunity, antioxidation, lowering blood lipids, and adsorbing mycotoxins, as well as its applications in the production of oligosaccharides, bio emulsifiers, nutritious and healthy foods, fruit preservation, animal nutrition, and wine production. Finally, research progress on the synthesis pathways of N-glycosylation and O-glycosylation in yeast mannoprotein and strategies for controlled gene modifications provide new technologies for efficient production of mannoprotein. Despite these advances, the production and application of yeast mannoprotein still face challenges. The diversified structures of yeast mannoprotein pose challenges to research. The action mechanism, spatial structure, molecular weight, and interrelationship of yeast mannoprotein are not fully understood. Future research should focus on elucidating the relationship between the structure of yeast mannoprotein and its biological activity. Combined with the application of biosynthesis technology, it is expected to promote the development of the yeast mannoprotein industry and enhance its applications in fields such as foods, cosmetics, medicines, etc.

Key words: yeast polysaccharides, yeast mannoprotein, biological activity, application, biosynthesis

摘要：

酵母甘露糖蛋白（mannoprotein）是一种位于酵母细胞壁最外层的非丝状糖蛋白，作为天然功能性成分，其商业化应用受限，目前仅用作葡萄酒稳定剂。本文简要介绍了其在肽链、核心区和外链组成方面的结构特征，并论述了酸法、碱法、酶法和物理方法提取酵母甘露糖蛋白的优缺点。还系统综述了酵母甘露糖蛋白在改善肠道健康、刺激免疫、抗氧化、降血脂、吸附霉菌毒素等方面的生物学活性，以及其在甘露寡糖生产、生物乳化剂、营养健康食品、水果保鲜、动物营养和葡萄酒中的应用。酵母甘露糖蛋白的N-糖基化和O-糖基化合成途径及过程控制基因改造策略的研究进展，为高效生产甘露糖蛋白提供了新技术，然而酵母甘露糖蛋白的生产结构多样化给研究带来了挑战，且结构-功能关系尚未揭示，未来应重点研究酵母甘露糖蛋白的结构与生物活性的关系，并结合生物合成技术，以推动其产业发展，提升在食品、化妆品和医药等领域的应用价值，推动酵母甘露糖蛋白的广泛商业化应用。

关键词: 酵母多糖, 酵母甘露糖蛋白, 生物活性, 应用, 生物合成

CLC Number:

SHENG Zhouhuang, CHEN Zhixian, ZHANG Yan. Research progress of yeast mannoproteins[J]. Synthetic Biology Journal, 2025, 6(2): 408-421.

盛周煌, 陈智仙, 张彦. 酵母甘露糖蛋白的研究进展[J]. 合成生物学, 2025, 6(2): 408-421.

Figures/Tables 2

Fig. 2 Structural characteristics of yeast mannoprotein(a—N-Glycosylated yeast mannoprotein;b—O-Glycosylated yeast mannoprotein)

Fig. 2 Biosynthetic pathway of yeast mannoprotein(Glu—Glucose; G6-P—Glucose-6-phosphat; PGM1—Phosphoglucomutase; G1-P—Glucose-1-phosphat; UGP1—Uridine diphosphate glucose pyrophosphatase; UDP-Glu—Uridine diphosphate glucose; PGI1—Phosphoglucose isomerase; F6-P—Fructose-6-phosphate;M6-P—Mannose-6-phosphate; PMI40—Mannose phosphate isomerase; SEC53—Phosphomannomutase; M1-P—Mannose-1-phosphate; PSA1—Guanosine diphosphate mannose pyrophosphatase; GDP-Man—Guanosine diphosphate mannose; UDP-GlcNAc—Uridine diphosphate-N-acetylglucosamine; Dol-P—Dolichol phosphate; Alg—Glycosyltransferase; OST—Oligosaccharides transferase;G-Ⅰ/G-Ⅱ—α-Glucosidase; ERMan1—Endoplasmic reticulum mannosidase Ⅰ;MGAT—Mannosyl-glycoprotein-N-acetylglucosaminyltransferase; DPM—Dolichol phosphate mannose synthase; PMT—Protein O-mannosyltransferase)

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