2012
DOI: 10.1007/s00217-012-1719-6
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Purification and characterization of a novel serine protease compositain from compositae (Scorzonera hispanica L.)

Abstract: In this research, a protease from the compositae (Scorzonera hispanica L.) was extracted and puriWed through (NH 4 ) 2 SO 4 precipitation, CM-Sephadex and Sephacryl S200. At the end of puriWcation by gel Wltration on a Sephacryl S-200 column, 87.11-fold puriWcation was achieved. It was shown that puriWed enzyme was homogeneous in terms of SDS-PAGE with molecular mass estimate of 30 kDa. The enzyme named compositain depicted an optimal pH of 8.0 and was stable at pH 7.0-9.0, and its optimal temperature was at 5… Show more

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Cited by 9 publications
(3 citation statements)
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“…They are broadly classified into two major classes based on their ability to cleave N-or C-terminal peptide bonds (exopeptidases) or internal peptide bonds of the polypeptide chain (endopeptidases) [20]. On the bases of their active site and mechanism of catalysis, proteases can be divided into seven groups by the MEROPS database: serine proteases, cysteine (thiol) proteases, aspartic proteases, metalloproteases, threonine proteases, glutamic acid proteases and unknown proteases [21]. Proteases of microbial origin such as Alcalase, Neutrase, Flavourzyme are the most commonly enzymes used in producing protein hydrolysates, but others such as protease from plant (e.g., papain) and animal sources (digestive enzymes, e.g., pepsin and trypsin) are also used [12,14,17].…”
Section: Introductionmentioning
confidence: 99%
“…They are broadly classified into two major classes based on their ability to cleave N-or C-terminal peptide bonds (exopeptidases) or internal peptide bonds of the polypeptide chain (endopeptidases) [20]. On the bases of their active site and mechanism of catalysis, proteases can be divided into seven groups by the MEROPS database: serine proteases, cysteine (thiol) proteases, aspartic proteases, metalloproteases, threonine proteases, glutamic acid proteases and unknown proteases [21]. Proteases of microbial origin such as Alcalase, Neutrase, Flavourzyme are the most commonly enzymes used in producing protein hydrolysates, but others such as protease from plant (e.g., papain) and animal sources (digestive enzymes, e.g., pepsin and trypsin) are also used [12,14,17].…”
Section: Introductionmentioning
confidence: 99%
“…The type of the enzyme is the core factor affecting the performance of the hydrolysate, such as molecular weight distribution, amino acid distribution, and the residual intact protein amount, that affects their bioactivity. According to their dynamic sites and catalytic mechanism, these proteases are categorized into seven groups by the MEROPS database: glutamic acid, threonine, serine, aspartic, cysteine, Metallo, and unknown proteases (Nadaroglu & Demır, 2012). Microbial‐derived proteases, such as Neutrase, Flavourzyme, and Alcalase, are commonly used enzymes for the production of protein hydrolysates.…”
Section: Introductionmentioning
confidence: 99%
“…The many species within the genus Bacillus are potential to secrete some extracellular enzymes such as high amylase, proteases, xylanases and cellulases. So, they play an important role in many biotechnological processes (Demir et al 2011;Nadaroglu et al 2010;Nadaroglu and Demir 2012).…”
Section: Introductionmentioning
confidence: 99%