Enzymatic characterization of Bacillus licheniformis γ-glutamyltranspeptidase fused with N-terminally truncated forms of Bacillus sp. TS-23 α-amylase

Hu, Hui-Yu; Yang, Jia-Ci; Chen, Jiau-Hua; Chi, Meng-Chun; Lin, Long-Liu

doi:10.1016/j.enzmictec.2012.04.005

Cited by 7 publications

(2 citation statements)

References 59 publications

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“…Based on the migration rate, the molecular masses of bands 6 and 9 were calculated to be around 37.6 to 22.6 kDa, respectively. They were in reasonable agreement with the molecular masses of approximately 40.5 and 21.1 kDa for the large and small subunits of BlGGT as stated by Hu et al 22 In fact, BaGGT and BlGGT are GGTs from the same genus but different species, although they are both sold as food-grade glutaminase. Multiple sequence alignments of BaGGT (A0A4V7TPB1) and BlGGT (T5HVH5) showed that the identity between them was 69.37%.…”

Section: Identification Of Ggtsupporting

confidence: 88%

Increase of Kokumi γ-Glutamyl Peptides in Porcine Hemoglobin Hydrolysate Using Bacterial γ-Glutamyltransferase

Zhang

Lametsch

2022

J. Agric. Food Chem.

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The kokumi sensation of protein hydrolysates could be enhanced by γ-glutamylation through forming a series of γ-glutamyl di- and tri-peptides. In this study, porcine hemoglobin hydrolysate was γ-glutamylated using enzymes from Bacillus amyloliquefaciens (Ba) or Bacillus licheniformis (Bl), which are sold as glutaminases but identified as γ-glutamyltransferases (GGTs). To yield more γ-glutamyl peptides, reaction conditions were optimized in terms of GGT source (BaGGT and BlGGT), substrate concentration (10, 20, and 40%), reaction time (3, 6, 12, and 24 h), and glutamine supplementation (20, 40, and 80 mM). Results showed that both the GGTs had the highest transpeptidase activity at similar pH values but different temperatures. In addition, BaGGT had stronger catalytic ability to form γ-glutamyl dipeptides, while BlGGT was more capable to generate γ-Glu-Val-Gly. Adding glutamine was more efficient to obtain more target peptides than adjusting the hydrolysate concentration and reaction time. This study contributes to the valorization of animal side streams.

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Section: Identification Of Ggtsupporting

confidence: 88%

Increase of Kokumi γ-Glutamyl Peptides in Porcine Hemoglobin Hydrolysate Using Bacterial γ-Glutamyltransferase

Zhang

Lametsch

2022

J. Agric. Food Chem.

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“…Besides, the stabilizing effect definitely renders the BlGGT-catalyzed process more economical due to the high cost of enzyme production and purification [31]. Our previous studies have shown that the CD spectrum of BlGGT exhibits two strong peaks of negative ellipticity at 208 and 222 nm [37,42], an indication of substantial α-helical content. These spectrometric characteristics were essentially conserved in enzyme-osmolyte samples when the denaturation temperature was set at 40°C ( Fig.…”

Section: Prevention Of Blggt From Heat-induced Inactivation By Biologmentioning

confidence: 99%

Protective Effect of Biological Osmolytes against Heat- and Chaotropic Agent-Induced Denaturation of Bacillus licheniformis ��-Glutamyl Transpeptidase

Chi

Lin

et al. 2018

Journal of Microbiology and Biotechnology

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In the present study, the stabilizing effect of four different biological osmolytes on Bacillus licheniformis γ-glutamyl transpeptidase (BlGGT) was investigated. BlGGT appeared to be stable under temperatures below 40°C, but the enzyme retained less than 10% of its activity at 60°C. The tested osmolytes exhibited different degrees of effectiveness against temperature inactivation of BlGGT, and sucrose was found to be the most effective among these. The use of circular dichroism spectroscopy for studying the secondary structure of BlGGT revealed that the temperature-induced conformational change of the protein molecule could be prevented by the osmolytes. Consistently, the molecular structure of the enzyme was essentially conserved by the osmolytes at elevated temperatures as monitored by fluorescence spectroscopy. Sucrose was further observed to counteract guanidine hydrochloride (GdnHCl)and urea-induced denaturation of BlGGT. Taken together, we observed evidently that some well-known biological osmolytes, especially sucrose, make a dominant contribution to the structural stabilization of BlGTT.

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Effects of Sodium Dodecyl Sulfate on the Enzyme Catalysis and Conformation of a Recombinant γ-Glutamyltranspeptidase from Bacillus licheniformis

Chi¹,

Lu²,

Huang³

et al. 2023

Protein J

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Enzymatic characterization of Bacillus licheniformis γ-glutamyltranspeptidase fused with N-terminally truncated forms of Bacillus sp. TS-23 α-amylase

Cited by 7 publications

References 59 publications

Increase of Kokumi γ-Glutamyl Peptides in Porcine Hemoglobin Hydrolysate Using Bacterial γ-Glutamyltransferase

Increase of Kokumi γ-Glutamyl Peptides in Porcine Hemoglobin Hydrolysate Using Bacterial γ-Glutamyltransferase

Protective Effect of Biological Osmolytes against Heat- and Chaotropic Agent-Induced Denaturation of Bacillus licheniformis ��-Glutamyl Transpeptidase

Effects of Sodium Dodecyl Sulfate on the Enzyme Catalysis and Conformation of a Recombinant γ-Glutamyltranspeptidase from Bacillus licheniformis

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