Effect of pulsed electric field on assembly structure of α-amylase and pectin electrostatic complexes

Weiping Jin, Zhifeng Wang, Dengfeng Peng, Wangyang Shen, Zhenzhou Zhu, Shuiyuan Cheng, Bin Li, Qingrong Huang

Research output: Contribution to journalArticle

Abstract

Pulsed electric field (PEF) could change the charge distribution of proteins and polysaccharides and affect their interactions and complexes aggregation, but those influences are not enough evaluated. Here, the effects of PEF on the complexes of α-amylase and pectin driven by electrostatic binding were studied. Changes in molecular conformation of α-amylase and assembly structure of α-amylase/pectin complexes were orderly assessed by fluorescence, FTIR, DSC, enzyme activities, particle size, ζ-potential, CLSM, and SEM. After PEF treatment (E~20 kV/cm, texp~1 ms, and 5 cycles), the intrinsic fluorescence of α-amylase was quenched, the content of β-sheet increased, enzyme activities lose almost 80%, and the denatured temperature increased. Ζeta-potential of α-amylase/pectin complexes did not change significantly, but the particle size rose gradually. The particle revolution of α-amylase/pectin complexes was recorded by Turbiscan, and the size growth model fit the Allometric function well. Finally, the complexes of α-amylase and pectin after PEF treatment tended to the branched, ring, or circles-like shape.

Original languageEnglish (US)
Article number105547
JournalFood Hydrocolloids
Volume101
DOIs
StatePublished - Apr 2020

Fingerprint

Amylases
pulsed electric fields
Static Electricity
amylases
pectins
Electrostatics
Electric fields
Enzyme activity
Particle Size
particle size
Fluorescence
molecular conformation
Particle size
fluorescence
enzyme activity
Molecular Conformation
Charge distribution
Fourier Transform Infrared Spectroscopy
Enzymes
Polysaccharides

All Science Journal Classification (ASJC) codes

  • Food Science
  • Chemical Engineering(all)
  • Chemistry(all)

Keywords

  • Assembling behavior
  • Electrostatic interaction
  • Particles motion
  • Protein/Polysaccharide complex
  • Pulsed electric field

Cite this

Jin, Weiping ; Wang, Zhifeng ; Peng, Dengfeng ; Shen, Wangyang ; Zhu, Zhenzhou ; Cheng, Shuiyuan ; Li, Bin ; Huang, Qingrong. / Effect of pulsed electric field on assembly structure of α-amylase and pectin electrostatic complexes. In: Food Hydrocolloids. 2020 ; Vol. 101.
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abstract = "Pulsed electric field (PEF) could change the charge distribution of proteins and polysaccharides and affect their interactions and complexes aggregation, but those influences are not enough evaluated. Here, the effects of PEF on the complexes of α-amylase and pectin driven by electrostatic binding were studied. Changes in molecular conformation of α-amylase and assembly structure of α-amylase/pectin complexes were orderly assessed by fluorescence, FTIR, DSC, enzyme activities, particle size, ζ-potential, CLSM, and SEM. After PEF treatment (E~20 kV/cm, texp~1 ms, and 5 cycles), the intrinsic fluorescence of α-amylase was quenched, the content of β-sheet increased, enzyme activities lose almost 80{\%}, and the denatured temperature increased. Ζeta-potential of α-amylase/pectin complexes did not change significantly, but the particle size rose gradually. The particle revolution of α-amylase/pectin complexes was recorded by Turbiscan, and the size growth model fit the Allometric function well. Finally, the complexes of α-amylase and pectin after PEF treatment tended to the branched, ring, or circles-like shape.",
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Effect of pulsed electric field on assembly structure of α-amylase and pectin electrostatic complexes. / Jin, Weiping; Wang, Zhifeng; Peng, Dengfeng; Shen, Wangyang; Zhu, Zhenzhou; Cheng, Shuiyuan; Li, Bin; Huang, Qingrong.

In: Food Hydrocolloids, Vol. 101, 105547, 04.2020.

Research output: Contribution to journalArticle

TY - JOUR

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AU - Jin, Weiping

AU - Wang, Zhifeng

AU - Peng, Dengfeng

AU - Shen, Wangyang

AU - Zhu, Zhenzhou

AU - Cheng, Shuiyuan

AU - Li, Bin

AU - Huang, Qingrong

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