Comparison Study on Polysaccharide Fractions from Laminaria japonica: Structural Characterization and Bile Acid Binding Capacity

2017 ◽  
Vol 65 (44) ◽  
pp. 9790-9798 ◽  
Author(s):  
Jie Gao ◽  
Lianzhu Lin ◽  
Baoguo Sun ◽  
Mouming Zhao
Keyword(s):  
Bile Acid ◽  
Structural Characterization ◽  
Binding Capacity ◽  
Laminaria Japonica ◽  
Comparison Study ◽  
Bile Acid Binding

A comparison study on polysaccharides extracted from Laminaria japonica using different methods: structural characterization and bile acid-binding capacity

2017 ◽  
Vol 8 (9) ◽  
pp. 3043-3052 ◽  
Author(s):  
Jie Gao ◽  
Lianzhu Lin ◽  
Baoguo Sun ◽  
Mouming Zhao
Keyword(s):  
Bile Acid ◽  
Rheological Properties ◽  
Structural Characterization ◽  
Binding Capacity ◽  
Laminaria Japonica ◽  
Extraction Methods ◽  
Comparison Study ◽  
Bile Acid Binding

The structural characterization, rheological properties and bile acid-binding capacity of LP obtained by seven different extraction methods were investigated.

Bile acid binding capacity of fish protein hydrolysates from discard species of the West Mediterranean Sea

2015 ◽  
Vol 6 (4) ◽  
pp. 1261-1267 ◽  
Author(s):  
Raúl Pérez-Gálvez ◽  
Pedro J. García-Moreno ◽  
Rocío Morales-Medina ◽  
Antonio Guadix ◽  
Emilia M. Guadix
Keyword(s):  
Bile Acid ◽  
Mediterranean Sea ◽  
Binding Capacity ◽  
Protein Hydrolysates ◽  
Fish Protein ◽  
The West ◽  
Bile Acid Binding ◽  
Fish Protein Hydrolysates

Fish protein hydrolysates from six fish discard species in the West Mediterranean Sea were tested for theirin vitrobile acid binding capacity.

scholarly journals Protein Engineering of Mung Bean (Vigna radiata (L.) Wilczek) 8Sα Globulin with Lactostatin

2020 ◽  
Vol 10 (24) ◽  
pp. 8787
Author(s):  
Ma. Carla Gamis ◽  
Lawrence Yves Uy ◽  
Antonio Laurena ◽  
Wilma Hurtada ◽  
Mary Ann Torio
Keyword(s):  
Liquid Chromatography ◽  
Bile Acid ◽  
Protein Engineering ◽  
Mung Bean ◽  
Binding Capacity ◽  
Protein Structures ◽  
Bioactive Peptide ◽  
Wild Type ◽  
Cholesterol Lowering ◽  
Bile Acid Binding

Mung bean is a well-known good source of protein. To increase its bioactivity, economic value, and nutritional content as a functional food and food additive, lactostatin (IIAEK), a cholesterol-lowering bioactive peptide, was engineered into mung bean 8Sα globulin, a major storage protein. The results showed that the mutated 8Sα globulin has a significant bile acid binding capacity (cholesterol-lowering activity) up to 47.25%. Moreover, superimposed mutant (Mut2) and wild-type (Wt) 3D protein structures showed a 93–97% identity, indicating that the mutant proteins are stable. Ultra-performance liquid chromatography(UPLC)-based assay showed similar retention time for wild-type and mutant protein samples. Both IIAEK peptide standard and Mut2 digest had comparable baseline peaks corresponding to the same molecular size based on the liquid chromatography-mass spectrometry (LC-MS) data. A 573.36-Da mass spectrum was seen in Mut2, which indicates that Mut2 8Sα globulin has been successfully mutated and digested to release the bioactive peptide, IIAEK. In vitro bile acid binding capacity showed that the 6-h Wt and 12-h engineered protein (Mut2) digests had the highest activity. Lastly, potential allergenicity was checked in the Allergen Database for Food Safety (ADFS) and the AllerBase database, and the IIAEK peptide matched the Bos d 5 epitopes. This study provides a strong foundation and basis for mung bean nutrition improvement, development of cholesterol-lowering food supplements, and protein engineering of other food proteins.

In Vitro Bile Acid Binding Capacity of Wheat Bran with Different Particle Sizes

2017 ◽  
Vol 94 (4) ◽  
pp. 654-658 ◽  
Author(s):  
Chun-yan Li ◽  
Andrew L. Mense ◽  
Lauren R. Brewer ◽  
Chuan Lau ◽  
Yong-Cheng Shi
Keyword(s):  
Bile Acid ◽  
Wheat Bran ◽  
Binding Capacity ◽  
Particle Sizes ◽  
Bile Acid Binding
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