A Study of the Interaction, Morphology, and Structure in Trypsin-Epigallocatechin-3-Gallate Complexes

Liu, Jiayin; Ghanizadeh, Hossein; Li, Xinmao; Han, Zhengyuan; Qiu, Youwen; Zhang, Yao; Chen, Xiuling; Wang, Aoxue

doi:10.3390/molecules26154567

A Study of the Interaction, Morphology, and Structure in Trypsin-Epigallocatechin-3-Gallate Complexes

Journal Article · Wed Jul 28 00:00:00 EDT 2021 · Molecules

DOI:https://doi.org/10.3390/molecules26154567· OSTI ID:1826778

^[1]; ^[2]; Li, Xinmao ^[3]; ^[3]; Qiu, Youwen ^[4]; Zhang, Yao ^[4]; Chen, Xiuling ^[3]; ^[5]

Northeast Agricultural Univ., Harbin (China). College of Horticulture and Landscape Architecture. College of Arts and Sciences
Massey Univ., Palmerston North (New Zealand). School of Agriculture and Environment
Northeast Agricultural Univ., Harbin (China). College of Horticulture and Landscape Architecture
Northeast Agricultural Univ., Harbin (China). College of Life Sciences
Northeast Agricultural Univ., Harbin (China). College of Horticulture and Landscape Architecture. College of Life Sciences

Understanding the interaction between proteins and polyphenols is of significance to food industries. The aim of this research was to investigate the mode of aggregation for trypsin-EGCG (Epigallocatechin-3-gallate) complexes. For this, the complex was characterized by fluorescence spectroscopy, circular dichroism (CD) spectra, small-angel X-ray scattering (SAXS), and atomic force microscope (AFM) techniques. The results showed that the fluorescence intensity of trypsin-EGCG complexes decreased with increasing the concentration of EGCG, indicating that the interaction between trypsin and EGCG resulted in changes in the microenvironment around fluorescent amino acid residues. The results of CD analysis showed conformational changes in trypsin after binding with EGCG. The results from SAXS analysis showed that the addition of EGCG results in the formation of aggregates of trypsin-EGCG complexes, and increasing the concentration of EGCG resulted in larger aggregates. AFM images showed that the trypsin-EGCG complex formed aggregates of irregular ellipsoidal shapes with the size of about 200 × 400 × 200 nm, with EGCG interconnecting the trypsin particles. Overall, according to these results, it was concluded that the large aggregates of trypsin-EGCG complexes are formed from several small aggregates that are interconnected. The results of this study shed some light on the interaction between digestive enzymes and EGCG.

View Accepted Manuscript (DOE)

Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Organization:: USDOE Office of Science (SC)

OSTI ID:: 1826778

Journal Information:: Molecules, Journal Name: Molecules Journal Issue: 15 Vol. 26; ISSN 1420-3049

Publisher:: MDPICopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
EGCG
aggregates
polyphenols
small-angel X-ray scattering
trypsin

A Study of the Interaction, Morphology, and Structure in Trypsin-Epigallocatechin-3-Gallate Complexes

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