Structural and functional properties of the glycosylated products of perilla seed meal proteins

Fructose (FRU), dextran (DEX), and maltodextrin (MD) with different molecular weights were used as inducers to modify perilla seed meal protein (PSMP) using a wet heating method, in order to explore their effects on the structural and functional properties of PSMP glycosylated products. The detectio...

Full description

Saved in:
Bibliographic Details
Main Authors: WANG Dan, LI He, ZHANG Zhijun, LI Huizhen
Format: Article
Language:English
Published: Zhejiang University Press 2023-08-01
Series:浙江大学学报. 农业与生命科学版
Subjects:
Online Access:https://www.academax.com/doi/10.3785/j.issn.1008-9209.2023.03.101
Tags: Add Tag
No Tags, Be the first to tag this record!
_version_ 1839607897293586432
author WANG Dan
LI He
ZHANG Zhijun
LI Huizhen
author_facet WANG Dan
LI He
ZHANG Zhijun
LI Huizhen
author_sort WANG Dan
collection DOAJ
description Fructose (FRU), dextran (DEX), and maltodextrin (MD) with different molecular weights were used as inducers to modify perilla seed meal protein (PSMP) using a wet heating method, in order to explore their effects on the structural and functional properties of PSMP glycosylated products. The detection results of grafting degree and browning degree showed that all three kinds of sugars underwent glycosylation reactions with PSMP. Compared with PSMP, the solubility of the three PSMP glycosylated products was improved under medium and alkaline conditions, with the solubility of P-DEX showing an increase of about 9% at pH 7.0. Meanwhile, the emulsifying, foaming, thermal properties, and oil-holding capacity of the three PSMP glycosylated products were significantly improved, with P-DEX showing the best performance. The detection results of Fourier transform infrared spectrum (FTIR) and endogenous fluorescence spectra confirmed that both the secondary and tertiary structures of PSMP glycosylated products were altered. The internal conformational unfolding of the modified products was observed by scanning electron microscopy (SEM), indicating that the structural changes were the main reason for the functional properties of the proteins. In summary, the glycosylation of PSMP significantly improved both its structural and functional properties. This study offers new ideas and methods for the applications of PSMP, as well as some theoretical and practical support for research into the structural relationships of glycosylated proteins.
format Article
id doaj-art-22e7df3159d24f73ba6c009f514be3a2
institution Matheson Library
issn 1008-9209
2097-5155
language English
publishDate 2023-08-01
publisher Zhejiang University Press
record_format Article
series 浙江大学学报. 农业与生命科学版
spelling doaj-art-22e7df3159d24f73ba6c009f514be3a22025-08-01T03:50:47ZengZhejiang University Press浙江大学学报. 农业与生命科学版1008-92092097-51552023-08-014955756510.3785/j.issn.1008-9209.2023.03.10110089209Structural and functional properties of the glycosylated products of perilla seed meal proteinsWANG DanLI HeZHANG ZhijunLI HuizhenFructose (FRU), dextran (DEX), and maltodextrin (MD) with different molecular weights were used as inducers to modify perilla seed meal protein (PSMP) using a wet heating method, in order to explore their effects on the structural and functional properties of PSMP glycosylated products. The detection results of grafting degree and browning degree showed that all three kinds of sugars underwent glycosylation reactions with PSMP. Compared with PSMP, the solubility of the three PSMP glycosylated products was improved under medium and alkaline conditions, with the solubility of P-DEX showing an increase of about 9% at pH 7.0. Meanwhile, the emulsifying, foaming, thermal properties, and oil-holding capacity of the three PSMP glycosylated products were significantly improved, with P-DEX showing the best performance. The detection results of Fourier transform infrared spectrum (FTIR) and endogenous fluorescence spectra confirmed that both the secondary and tertiary structures of PSMP glycosylated products were altered. The internal conformational unfolding of the modified products was observed by scanning electron microscopy (SEM), indicating that the structural changes were the main reason for the functional properties of the proteins. In summary, the glycosylation of PSMP significantly improved both its structural and functional properties. This study offers new ideas and methods for the applications of PSMP, as well as some theoretical and practical support for research into the structural relationships of glycosylated proteins.https://www.academax.com/doi/10.3785/j.issn.1008-9209.2023.03.101perilla seed meal proteinglycosylationstructureemulsifying propertyfunctional properties
spellingShingle WANG Dan
LI He
ZHANG Zhijun
LI Huizhen
Structural and functional properties of the glycosylated products of perilla seed meal proteins
浙江大学学报. 农业与生命科学版
perilla seed meal protein
glycosylation
structure
emulsifying property
functional properties
title Structural and functional properties of the glycosylated products of perilla seed meal proteins
title_full Structural and functional properties of the glycosylated products of perilla seed meal proteins
title_fullStr Structural and functional properties of the glycosylated products of perilla seed meal proteins
title_full_unstemmed Structural and functional properties of the glycosylated products of perilla seed meal proteins
title_short Structural and functional properties of the glycosylated products of perilla seed meal proteins
title_sort structural and functional properties of the glycosylated products of perilla seed meal proteins
topic perilla seed meal protein
glycosylation
structure
emulsifying property
functional properties
url https://www.academax.com/doi/10.3785/j.issn.1008-9209.2023.03.101
work_keys_str_mv AT wangdan structuralandfunctionalpropertiesoftheglycosylatedproductsofperillaseedmealproteins
AT lihe structuralandfunctionalpropertiesoftheglycosylatedproductsofperillaseedmealproteins
AT zhangzhijun structuralandfunctionalpropertiesoftheglycosylatedproductsofperillaseedmealproteins
AT lihuizhen structuralandfunctionalpropertiesoftheglycosylatedproductsofperillaseedmealproteins