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Related Concept Videos

Protein Buffers in Blood Plasma and Cells01:20

Protein Buffers in Blood Plasma and Cells

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The human body utilizes protein buffer systems to maintain a stable pH. These systems capitalize on the dual role of amino acids, which can act as acids or bases by accepting or releasing hydrogen ions in response to pH changes. Protein buffer systems are particularly significant in the extracellular fluid (ECF) and intracellular fluid (ICF) of active cells, where structural and functional proteins provide substantial buffering capacity.
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pH01:24

pH

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The potential of hydrogen (pH) is a measure of the acidity or basicity of a water-based solution determined by the concentration of hydronium ions (H3O+). In one liter of pure water at neutral pH, there are 1×10−7 moles of hydronium ions. However, the extensive range of hydronium ion concentrations present in water-based solutions makes measuring pH in moles cumbersome. Therefore, a pH scale was developed to convert moles of hydronium ions into the negative logarithm of the hydronium...
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Stomach pH Regulation01:21

Stomach pH Regulation

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The human body carefully regulates the internal pH of different organs to maintain homeostasis. For example, while the blood plasma maintains a neutral pH of 7, the stomach lumen has an acidic pH of 1.5 - 3.5. The low pH of stomach lumen helps kill pathogens in the food and break down complex food molecules.
The acid-secreting gastric mucosal epithelial cells (parietal cells) lining the stomach lumen maintain the low pH in the lumen. Numerous ion transporters and channels on these parietal...
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Extraction: Effects of pH00:53

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Consider a neutral form of an amine, B, with a partition coefficient, K, in a liquid mixture containing organic and aqueous phases. The pH of the aqueous phase affects the charge on acidic and basic solutes, and the charged form is usually more soluble in the aqueous phase. Suppose the conjugate acid form of the amine is soluble only in the aqueous phase while the base form is soluble in both phases. Then the distribution coefficient, D, can be given as the ratio of amine concentration in the...
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pH Scale02:41

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Hydronium and hydroxide ions are present both in pure water and in all aqueous solutions, and their concentrations are inversely proportional as determined by the ion product of water (Kw). The concentrations of these ions in a solution are often critical determinants of the solution’s properties and the chemical behaviors of its other solutes. Two different solutions can differ in their hydronium or hydroxide ion concentrations by a million, billion, or even trillion times. A common means of...
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Protein Denaturation01:28

Protein Denaturation

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The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
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Physical Processing-Assisted pH Shifting for Food Protein Modification: A Comprehensive Review.

Ruiqi Long1,2, Yuanyuan Huang1,2, Mokhtar Dabbour3

  • 1School of Food and Biological Engineering, Jiangsu University, 301 Xuefu Road, Zhenjiang 212013, China.

Foods (Basel, Switzerland)
|July 12, 2025
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Summary

Combining pH shifting with physical methods like ultrasound or high-pressure processing enhances protein functionality. This eco-efficient strategy improves sustainable protein sources, reducing reliance on extreme conditions for food development.

Keywords:
conformational attributespH shiftingplant proteinsolubilityultrasonication

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Area of Science:

  • Food Science and Technology
  • Biotechnology
  • Sustainable Agriculture

Background:

  • Growing demand for sustainable protein sources necessitates efficient processing of traditional and novel proteins (plant-based, algae).
  • pH shifting is a cost-effective method for altering protein structure and functionality.
  • Extreme pH conditions can cause protein denaturation and undesirable by-products.

Purpose of the Study:

  • To review the integration of pH shifting with physical processing techniques for protein modification.
  • To highlight the impact of combined treatments on protein conformation and functionality.
  • To assess the sustainability and eco-efficiency of these combined approaches in industrial applications.

Main Methods:

  • Integration of pH shifting with physical processing: ultrasound, high-pressure processing, pulsed electric fields, and thermal treatments.
  • Analysis of protein conformational transitions induced by combined treatments.
  • Evaluation of functional properties: solubility, emulsification, foaming capacity, and thermal stability.

Main Results:

  • Combined treatments effectively modify protein structure and enhance functional properties.
  • These integrated methods reduce the need for extreme acidic or alkaline conditions.
  • Improved protein functionality supports the development of sustainable and nutritious food products.

Conclusions:

  • Integrated pH shifting and physical processing offer a promising, eco-efficient strategy for protein modification.
  • This approach enhances the utilization of sustainable protein sources, particularly from plants and algae.
  • Milder processing conditions preserve nutritional quality and functional attributes, aligning with sustainable food development goals.