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  1. Article ; Online: Effects of freezing and drying programs on IgY aggregation and activity during microwave freeze-drying: Protective effects and interactions of trehalose and mannitol.

    Wang, Zhe / Liu, Wenchao / Duan, Xu / Ren, Guangyue / Li, Linlin / Cao, Weiwei / Guo, Jingfang / Jiao, Xueyuan / Zhu, Lewen / Wei, Xinyu

    International journal of biological macromolecules

    2024  Volume 260, Issue Pt 1, Page(s) 129448

    Abstract: The acquisition of high quality lyophilized IgY products, characterized by an aesthetically pleasing visage, heightened stability, and a marked preservation of activity, constitutes an indispensable pursuit in augmenting the safety and pragmatic utility ... ...

    Abstract The acquisition of high quality lyophilized IgY products, characterized by an aesthetically pleasing visage, heightened stability, and a marked preservation of activity, constitutes an indispensable pursuit in augmenting the safety and pragmatic utility of IgY. Within this context, an exploration was undertaken to investigate an innovative modality encompassing microwave freeze-drying (MFD) as a preparatory methodology of IgY. Morphological assessments revealed that both cryogenic freezing and subsequent MFD procedures resulted in aggregation of IgY, with the deleterious influence posed by the MFD phase transcending that of the freezing phase. The composite protective agent comprised of trehalose and mannitol engendered a safeguarding effect on the structural integrity of IgY, thereby attenuating reducing aggregation between IgY during the freeze-drying process. Enzyme-linked immunosorbent assay (ELISA) outcomes demonstrated a discernible correlation between IgY aggregation and a notable reduction in its binding affinity towards the pertinent antigen. Comparative analysis vis-à-vis the control sample delineated that when the trehalose-to-mannitol ratio was upheld at 1:3, a two-fold outcome was achieved: a mitigation of the collapse susceptibility within the final product as well as a deterrence of IgY agglomeration, concomitant with an elevated preservation rate of active antibodies (78.57 %).
    MeSH term(s) Freezing ; Trehalose/pharmacology ; Trehalose/chemistry ; Mannitol/chemistry ; Freeze Drying/methods ; Immunoglobulins
    Chemical Substances Trehalose (B8WCK70T7I) ; Mannitol (3OWL53L36A) ; IgY ; Immunoglobulins
    Language English
    Publishing date 2024-01-14
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2024.129448
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: A comprehensive review on stability of therapeutic proteins treated by freeze-drying: induced stresses and stabilization mechanisms involved in processing

    Wang, Zhe / Li, Linlin / Ren, Guangyue / Duan, Xu / Guo, Jingfang / Liu, Wenchao / Ang, Yuan / Zhu, Lewen / Ren, Xing

    Drying Technology. 2022 Dec. 12, v. 40, no. 16 p.3373-3388

    2022  

    Abstract: Therapeutic protein preparations are usually stored in a solid state to reduce the physical and chemical degradation by removing most of the solvent (mostly water) in liquid protein preparations, improving stability and maintaining biological activity. ... ...

    Abstract Therapeutic protein preparations are usually stored in a solid state to reduce the physical and chemical degradation by removing most of the solvent (mostly water) in liquid protein preparations, improving stability and maintaining biological activity. Freeze-drying (FD) is a common method to produce the dehydrated therapeutic protein. However, various induced stresses exist in the processing steps involved in FD, such as freezing process, primary drying, and secondary drying, may cause protein instability. To overcome this problem, two means are often employed: adding stabilizers to protect proteins from physical damage associated with the FD process; optimizing parameter conditions during the FD process to reduce protein degeneration. Therefore, a deep understanding of the protein preparation formula composition and FD process parameters is crucial for the development of stable therapeutic protein products. This study reviewed the stabilization mechanisms of protein during FD, focused on the factors that induce protein instability, and discussed the relationship between protein structure changes and instability, expected to provide references for solving the instability during protein freeze-drying and storage.
    Keywords bioactive properties ; chemical degradation ; freeze drying ; liquids ; protein structure ; solvents ; therapeutics ; Therapeutic protein ; lyophilization ; instability
    Language English
    Dates of publication 2022-1212
    Size p. 3373-3388.
    Publishing place Taylor & Francis
    Document type Article ; Online
    ZDB-ID 2049461-0
    ISSN 1532-2300 ; 0737-3937
    ISSN (online) 1532-2300
    ISSN 0737-3937
    DOI 10.1080/07373937.2022.2048847
    Database NAL-Catalogue (AGRICOLA)

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  3. Article ; Online: Improving effect of disaccharides and maltodextrin on preparation of egg yolk powder by microwave-assisted freeze-drying: Functional properties, structural properties, and retention rate of active IgY.

    Wang, Zhe / Duan, Xu / Ren, Guangyue / Guo, Jingfang / Ji, Jiangtao / Xu, Yiming / Cao, Weiwei / Li, Linlin / Zhao, Mengyue / Ang, Yuan / Jin, Xin / Bhandari, Bhesh / Zhu, Lewen / Zhang, Yan

    Food chemistry

    2022  Volume 404, Issue Pt A, Page(s) 134626

    Abstract: The preparation of egg yolk powder (EYP) with excellent solubility and high retention of active IgY is of great significance for increasing the added value and promoting the application of EYP. A new method of preparing EYP by microwave-assisted freeze- ... ...

    Abstract The preparation of egg yolk powder (EYP) with excellent solubility and high retention of active IgY is of great significance for increasing the added value and promoting the application of EYP. A new method of preparing EYP by microwave-assisted freeze-drying (MFD) was researched. Confocal laser scanning microscopy results demonstrated that the supplementation of excipients (sucrose, trehalose, and maltodextrin) could inhibit lipoproteins aggregation in egg yolk induced by freezing. Scanning electron microscopy indicated that drying further damaged the structure of lipoproteins in EYP, leading to lipid separation from it. FTIR and fluorescence spectra confirmed this finding, indicating that excipients enhance protein stability. Compared with conventional freeze-drying (FD), EYP prepared by MFD, particularly that containing excipients, had higher solubility (63 g/100 g), active antibody retention rate and shorter drying time. Therefore, excipients can significantly improve the solubility and stability of EYP and the retention rate of active IgY.
    MeSH term(s) Powders ; Egg Yolk ; Disaccharides ; Microwaves ; Excipients
    Chemical Substances Powders ; IgY ; Disaccharides ; maltodextrin (7CVR7L4A2D) ; Excipients
    Language English
    Publishing date 2022-10-18
    Publishing country England
    Document type Journal Article
    ZDB-ID 243123-3
    ISSN 1873-7072 ; 0308-8146
    ISSN (online) 1873-7072
    ISSN 0308-8146
    DOI 10.1016/j.foodchem.2022.134626
    Database MEDical Literature Analysis and Retrieval System OnLINE

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