Molecular forces governing protein-protein interaction: Structure-function relationship of complexes protein in the food industry

Alrosan, Mohammad; Tan, Thuan‐Chew; Easa, Azhar Mat; Gammoh, Sana; Alu’datt, Muhammad H.

doi:10.1080/10408398.2021.1871589

Cited by 47 publications

(39 citation statements)

References 131 publications

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“…Moreover, the protein complexes became more readily soluble in water after freeze‐drying. The amount of foreign proteins incorporated into protein complexes have been noted to play a major role in affecting the tertiary and secondary protein structure of the mixed protein complexes that are created (Wang et al ., 2019; Alrosan et al ., 2021b). It is noteworthy that when the ratio of LP‐QP was less than 1:1, the LP‐QP protein complexes showed large amounts of precipitation that could be visually detected without centrifugation (data not shown).…”

Section: Resultsmentioning

confidence: 99%

“…Solubility is one of the most significant functional properties upon which other functional properties depend (Alrosan et al ., 2021b). Accordingly, substantial efforts have concentrated on the solubility of proteins in the preparation of soluble biopolymer composites (Wang et al ., 2019; He et al ., 2020).…”

Section: Introductionmentioning

confidence: 99%

“…Non‐covalent forces including hydrophobic and electrostatic interactions as well as hydrogen bonds play a role in determining protein solubility. Hydrophobic interactions in aqueous solutions enable protein–protein interactions (PPIs) that can affect the solubility of protein such as QPs (Alrosan et al ., 2021b). The exposure of hydrophobic amino acids between non‐polar protein groups during PPI leads to an increase in protein solubility (Pearce & Kinsella, 1978; Lawal & Adebowale, 2004).…”

Section: Introductionmentioning

confidence: 99%

“…Various approaches have been employed towards improving the functional properties of plant proteins (Sun et al ., 2018; Wang et al ., 2018; He et al ., 2020; Zheng et al ., 2020; Alrosan et al ., 2021b). The induction of PPI is one of the best strategies for enhancing the functionality of plant proteins (Lin et al ., 2017; Alrosan et al ., 2021a).…”

Section: Introductionmentioning

confidence: 99%

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Mechanisms of molecular and structural interactions between lentil and quinoa proteins in aqueous solutions induced by pH recycling

Alrosan

Tan

Easa

et al. 2021

Int J of Food Sci Tech

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There has been a growing interest in plant proteins due to their beneficial health effects, low cost and variety of applications in food industries. The low solubility of lentil proteins (LPs) is one of the significant factors that limit their use in food applications. Quinoa proteins (QPs), which have high water solubility, were combined with LPs at pH 12 to generate LP-QP complexes to generate pH-based soluble protein compounds. The LP-QP complexes demonstrated a large surface charge with an increase solubilisation of the protein complexes by more than 85%, together with resistance to protein aggregation. The combination of LPs to QPs led to a significant increase (P < 0.05) in unique tertiary and secondary protein structures as determined by the protein-protein interaction (PPI) technique involving pH recycling. Interactions between LPs and QPs affected the surface morphology of the protein complexes formed. Electrostatic interactions, hydrophobic forces and hydrogen bonding were indicated to play key roles in the PPIs. The capacity of pH cycling to illustrate the above protein interactions shows that this is a robust approach for assessing the emulsion and foaming properties of food proteins.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Mechanisms of molecular and structural interactions between lentil and quinoa proteins in aqueous solutions induced by pH recycling

Alrosan

Tan

Easa

et al. 2021

Int J of Food Sci Tech

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show abstract

“…Molecular forces play a major role in PPI (Alrosan et al, 2021b); hence, it should be investigated in this study. Consequently, thiourea, SDS, and NaCl (10 mM) were added to the protein samples as foreign substances.…”

Section: Protein Interaction Between Lps and Wpismentioning

confidence: 99%

Mechanism of the structural interaction between whey and lentil proteins in the unique creation of a protein structure

Alrosan

Tan

Easa

et al. 2021

Journal of Food Science

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Poor solubility is a substantial factor that restricts the production of high value-added lentil proteins (LPs). In this study, whey protein isolates (WPIs), which have high solubility and are used in various food industries, were mixed with LPs at pH 12 to create LP-WPI protein complexes with improved water solubility properties using pH-recycling approach (maintained at pH 12.0 for 60 min and then readjusting to pH 7.0). LP-WPI protein complexes produced in this study have gained high surface charge, increased in the solubilization of protein complexes to ≈92%, as well as improved resistance against protein aggregation. The ratio of LPs to WPIs has a significant effect on the generation of unique tertiary and secondary protein structures based on the protein-protein interaction (PPI) technique via pH-recycling. The protein interaction between LPs and WPIs resulted in alteration on the surface morphology of the produced protein complexes. This study showed that electrostatic interaction, hydrophobic force, and hydrogen bond appear as major molecular forces in this PPI. The efficacy of the pH-recycling method used in this research indicates that this approach could be a robust approach to enhance the functional properties of food proteins. K E Y W O R D Slentil proteins, molecular forces, solubility, structural interactions, whey protein isolates Practical Application: The pH-recycling technique is a proven technique for protein complexation in creating novel protein complexes with improved functional properties. Even though lentils are a rich source of plant-based protein, its utilization by food industries is restricted due to the poor water solubility of lentil proteins (LPs). However, by using complexing lentil proteins with whey protein isolates (WPIs), that is, LP-WPI protein complex, was developed. The water solubility of LP-WPI protein complex was significantly higher than LPs, up to approximately 92%. In addition, this could improve the utilization of lentil seeds in food application as an alternative for animal-based proteins.

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Infrared Spectroscopy of SARS‐CoV‐2 Viral Protein: from Receptor Binding Domain to Spike Protein

Mancini,

Macis,

Mosetti

et al. 2024

Advanced Science

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Spike (S) glycoprotein is the largest structural protein of SARS‐CoV‐2 virus and the main one involved in anchoring of the host receptor ACE2 through the receptor binding domain (RBD). S protein secondary structure is of great interest for shedding light on various aspects, from functionality to pathogenesis, finally to spectral fingerprint for the design of optical biosensors. In this paper, the secondary structure of SARS‐CoV‐2 S protein and its constituting components, namely RBD, S1 and S2 regions, are investigated at serological pH by measuring their amide I infrared absorption bands through Attenuated Total Reflection Infrared (ATR‐IR) spectroscopy. Experimental data in combination with MultiFOLD predictions, Define Secondary Structure of Proteins (DSSP) web server and Gravy value calculations, provide a comprehensive understanding of RBD, S1, S2, and S proteins in terms of their secondary structure content, conformational order, and interaction with the solvent.

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Molecular forces governing protein-protein interaction: Structure-function relationship of complexes protein in the food industry

Cited by 47 publications

References 131 publications

Mechanisms of molecular and structural interactions between lentil and quinoa proteins in aqueous solutions induced by pH recycling

Mechanisms of molecular and structural interactions between lentil and quinoa proteins in aqueous solutions induced by pH recycling

Mechanism of the structural interaction between whey and lentil proteins in the unique creation of a protein structure

Infrared Spectroscopy of SARS‐CoV‐2 Viral Protein: from Receptor Binding Domain to Spike Protein

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