Heterologous expression of protein-glutaminase in Escherichia coli Nissle 1917 for improved flavor properties of soy protein and its implications on high-moisture extrudates

Li, Jiaming; Zhang, Xinwen; Luo, Shijun; Wu, Xinhong; Zhang, Guoqiang; Li, Jianghua; Liu, Xiao

doi:10.1016/j.fbio.2024.103591

Food Bioscience

2024

DOI: 10.1016/j.fbio.2024.103591

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Heterologous expression of protein-glutaminase in Escherichia coli Nissle 1917 for improved flavor properties of soy protein and its implications on high-moisture extrudates

Jiaming Li,

Xinwen Zhang,

Shijun Luo

et al.

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Cited by 4 publications

References 34 publications

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Engineering of protein glutaminase for highly efficient modification of fish myofibrillar protein through structure-based and computational-aided strategy

Leng,

Li,

Liang

et al. 2024

Food Chemistry

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Engineering of protein glutaminase for highly efficient modification of fish myofibrillar protein through structure-based and computational-aided strategy

Leng,

Li,

Liang

et al. 2024

Food Chemistry

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Novel aptasensor based on polyaniline functionalized carboxylated dobby carbon nanotubes and molybdenum disulfide for endotoxin detection

Wang,

Yan,

Shen

et al. 2024

Talanta

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Functional and Mechanistic Dissection of Protein Glutaminase PG3 and Its Rational Engineering for Enhanced Modification of Myofibrillar Proteins

Leng,

Li,

Yuan

et al. 2024

J. Agric. Food Chem.

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Protein glutaminases (PG; EC = 3.5.1.44) are enzymes known for enhancing protein functionality. In this study, we cloned and expressed the gene chryb3 encoding protein glutaminase PG3, exhibiting 39.4 U/mg specific activity. Mature-PG3 featured a substrate channel surrounded by aromatic and hydrophobic amino acids at positions 38−45 and 78−84, with Val81 playing a pivotal role in substrate affinity. The dynamic opening and closing motions between Gly65, Thr66, and Cys164 at the catalytic cleft greatly influence substrate binding and product release. Redesigning catalytic pocket and cocatalytic region produced combinatorial mutant MT6 showing a 2.69-fold increase in specific activity and a 2.99-fold increase at t 65 °C1/2 . Furthermore, MT6 boosted fish myofibrillar protein (MP) solubility without NaCl. Key residues such as Thr3, Asn54, Val81, Tyr82, Asn107, and Ser108 were vital for PG3-myosin interaction, particularly Asn54 and Asn107. This study sheds light on the catalytic mechanism of PG3 and guided its rational engineering and utilization in low-salt fish MP product production.

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Heterologous expression of protein-glutaminase in Escherichia coli Nissle 1917 for improved flavor properties of soy protein and its implications on high-moisture extrudates

Cited by 4 publications

References 34 publications

Engineering of protein glutaminase for highly efficient modification of fish myofibrillar protein through structure-based and computational-aided strategy

Engineering of protein glutaminase for highly efficient modification of fish myofibrillar protein through structure-based and computational-aided strategy

Novel aptasensor based on polyaniline functionalized carboxylated dobby carbon nanotubes and molybdenum disulfide for endotoxin detection

Functional and Mechanistic Dissection of Protein Glutaminase PG3 and Its Rational Engineering for Enhanced Modification of Myofibrillar Proteins

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