Weichun Pan , Zhe Li , Weiwei Tu , Xinyu Hu , Jinlai Yang , Ying Gao , Huimin Yang , Christos Ritzoulisa , Fuge Niu , Liangru Wu
{"title":"Characterizations of protein extracted from Moso bamboo shoot","authors":"Weichun Pan , Zhe Li , Weiwei Tu , Xinyu Hu , Jinlai Yang , Ying Gao , Huimin Yang , Christos Ritzoulisa , Fuge Niu , Liangru Wu","doi":"10.1016/j.ijbiomac.2025.140897","DOIUrl":null,"url":null,"abstract":"<div><div>Low economic returns limit the widespread cultivation of bamboo, which could otherwise offer solutions to several global needs. This study aims to explore the physicochemical properties of nanoparticles (NPs) in protein solutions extracted from <em>Moso</em> bamboo shoots to enhance bamboo shoot applications. A 10 kDa molecular weight cutoff filter is used for protein purification, while amino acid composition analysis, SDS-PAGE, three independent spectroscopic techniques, and light scattering are employed for characterization. The purified protein was found to consist of 18 amino acids with molecular weights spreading from 30 kDa to 50 kDa. The corresponding secondary structure was also evaluated: Coiled, poly-dispersed NPs exhibited negative surface charges with sizes of ca 100 nm. ρ-Ratio decreases upon dilution operation, indicating the NPs' topology variation. Stability studies reveal that the NPs were temperature-sensitive, and electrostatic interactions between protein molecules play a key role in regulating the size and shape of the NPs.</div></div>","PeriodicalId":333,"journal":{"name":"International Journal of Biological Macromolecules","volume":"304 ","pages":"Article 140897"},"PeriodicalIF":7.7000,"publicationDate":"2025-02-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"International Journal of Biological Macromolecules","FirstCategoryId":"92","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0141813025014461","RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
Low economic returns limit the widespread cultivation of bamboo, which could otherwise offer solutions to several global needs. This study aims to explore the physicochemical properties of nanoparticles (NPs) in protein solutions extracted from Moso bamboo shoots to enhance bamboo shoot applications. A 10 kDa molecular weight cutoff filter is used for protein purification, while amino acid composition analysis, SDS-PAGE, three independent spectroscopic techniques, and light scattering are employed for characterization. The purified protein was found to consist of 18 amino acids with molecular weights spreading from 30 kDa to 50 kDa. The corresponding secondary structure was also evaluated: Coiled, poly-dispersed NPs exhibited negative surface charges with sizes of ca 100 nm. ρ-Ratio decreases upon dilution operation, indicating the NPs' topology variation. Stability studies reveal that the NPs were temperature-sensitive, and electrostatic interactions between protein molecules play a key role in regulating the size and shape of the NPs.
期刊介绍:
The International Journal of Biological Macromolecules is a well-established international journal dedicated to research on the chemical and biological aspects of natural macromolecules. Focusing on proteins, macromolecular carbohydrates, glycoproteins, proteoglycans, lignins, biological poly-acids, and nucleic acids, the journal presents the latest findings in molecular structure, properties, biological activities, interactions, modifications, and functional properties. Papers must offer new and novel insights, encompassing related model systems, structural conformational studies, theoretical developments, and analytical techniques. Each paper is required to primarily focus on at least one named biological macromolecule, reflected in the title, abstract, and text.