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| Braz,Vânia S.; Lang,Elza A.S.; Marques,Marilis V.. |
| The metallopeptidases have a very important role in bacteria, being involved in several processes that rely on protein turnover, such as nutrition, degradation of signal peptides, protein localization and virulence. We have cloned and characterized the gene of the metalloendopeptidase PepF from the aquatic bacterium Caulobacter crescentus. The gene upstream of pepF (orf1) encodes a conserved hypothetical protein found in Mycobacterium and Streptomyces. pepF is co-transcribed with the gene downstream (orf3), which encodes a protein that belongs to the ABC1 protein kinase family, suggesting that these two proteins may share a common function in the cell. The C. crescentus PepF protein possesses the conserved HEXGH motif present in zinc binding domains of... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Endopeptidase; M3 family; Gene regulation; Bacteria. |
| Ano: 2002 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822002000100017 |
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| SBROGGIO,Melissa Ferreira; MONTILHA,Marina Silveira; FIGUEIREDO,Vitória Ribeiro Garcia de; GEORGETTI,Sandra Regina; KUROZAWA,Louise Emy. |
| Abstract The objective of this work was to evaluate the antioxidant activity of protein hydrolysates obtained by the enzymatic hydrolysis of okara using an endopeptidase (Alcalase) and exopeptidase (Flavourzyme). The reaction was monitored by the pH-stat procedure in which five aliquots were collected during the hydrolysis by each enzyme, corresponding to different degrees of hydrolysis (DH). The antioxidant activities of the aliquots were evaluated by the ABTS, DPPH and FRAP methods. For the hydrolysates obtained using Alcalase, the antioxidant activities increased from: 68.6 to 99.5% (ABTS), 14.5 to 17.7% (DPPH) and 222.6 to 684.9 µM Trolox (FRAP), when the DH varied from 0 to 33.6%. With respect to Flavourzyme, the results were: 67.2 to 88.2% (ABTS),... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Soy pulp; Endopeptidase; Exopeptidase; Antioxidant capacity; Bioactive peptides. |
| Ano: 2016 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612016000200375 |
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| Sobottka,Andréa Michel; Tonial,Fabiana; Sytwala,Sonja; Melzig,Matthias. |
| In the family of Euphorbiaceae,the genera Euphorbia and Sapium are known to contain essentially latex-bearing species. In the present study, the latex of Euphorbia selloi(Klotzsch & Garcke) Boiss., Euphorbia papillosa A.St.-Hil., and Sapium glandulosum (L.) Morong, plants native from Brazil, were examined concerning proteolytic activity. All studied species have proteins with significant proteolytic activity and E. papillosa has the greatest specific activity. Aiming to verify the type of protease present, an assay with different inhibitors was performed. In the three tested plants, the proteolytic activity was significantly inhibited by a serine protease inhibitor 4-(2-aminoethyl)-benzenesulfonyl fluoride hydrochloride (AEBSF). Using techniques of... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Euphorbiaceae/species/phytochemistry; Euphorbia papillosa/phytochemistry; Euphorbia selloi/phytochemistry; Sapium glandulosum/phytochemistry; Euphorbia papillosa/proteinase activity; Euphorbia selloi/proteinase activity; Sapium glandulosum/proteinase activity; Endopeptidase; Gel electrophoresis. |
| Ano: 2014 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1984-82502014000300559 |
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| Hsiao,Nai-Wan; Chen,Yeh; Kuan,Yi-Chia; Lee,Yen-Chung; Lee,Shuo-Kang; Chan,Hsin-Hua; Kao,Chao-Hung. |
| Background Aspartic proteases are a subfamily of endopeptidases that are useful in a variety of applications, especially in the food processing industry. Here we describe a novel aspartic protease that was purified from Peptidase R, a commercial protease preparation derived from Rhizopus oryzae. Results An aspartic protease sourced from Peptidase R was purified to homogeneity by anion exchange chromatography followed by polishing with a hydrophobic interaction chromatography column, resulting in a 3.4-fold increase in specific activity (57.5 × 10³ U/mg) and 58.8% recovery. The estimated molecular weight of the purified enzyme was 39 kDa. The N-terminal sequence of the purified protein exhibited 63-75% identity to rhizopuspepsins from various Rhizopus... |
| Tipo: Journal article |
Palavras-chave: Chromatography; Endopeptidase; Food processing industry; Homogeneity; Rhizopuspepsin. |
| Ano: 2014 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582014000200006 |
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