Safety Evaluation of Amino Peptidase Enzyme Preparation derived from Aspergillus niger

Coenen, T.M.M.; Aughton, P

doi:10.1016/s0278-6915(98)00041-6

Cited by 7 publications

(4 citation statements)

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“…Since A. niger strain NRRL 3112 was used as a source for the F-AP hydrolyzing activity in an enzyme preparation described previously (8), culture broth of this strain was used to purify a protein with high activity towards F-pNA. The N-terminal sequences were determined for the N-terminal end of the mature protein and for two peptides of a tryptic digest thereof.…”

Section: Resultsmentioning

confidence: 99%

“…Experiments have shown that a particular enzyme preparation of A. niger that contains a specific aminopeptidase activity can liberate phenylalanine from proteins that are present in dough and (semi)hard cheeses (8), thereby improving the flavor and aroma of these products. So far, only one phenylalanine-specific aminopeptidase has been characterized, namely, APF1 from the basidiomycetous fungus Schizophyllum commune (6).…”

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confidence: 99%

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Aminopeptidase C of Aspergillus niger Is a Novel Phenylalanine Aminopeptidase

Basten

Dekker

Schaap

2003

Appl Environ Microbiol

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A novel enzyme with a specific phenylalanine aminopeptidase activity (ApsC) from Aspergillus niger (CBS 120.49) has been characterized. The derived amino acid sequence is not similar to any previously characterized aminopeptidase sequence but does share similarity with some mammalian acyl-peptide hydrolase sequences. ApsC was found to be most active towards phenylalanine ␤-naphthylamide (F-␤NA) and phenylalanine para-nitroanilide (F-pNA), but it also displayed activity towards other amino acids with aromatic side chains coupled to ␤NA; other amino acids with nonaromatic side chains coupled to either pNA or ␤NA were not hydrolyzed or were poorly hydrolyzed. ApsC was not able to hydrolyze N-acetylalanine-pNA, a substrate for acyl-peptide hydrolases.Many food products contain flavors obtained by the hydrolysis of proteins. These peptides and amino acids can taste sweet, sour, or bitter. Mixtures of endoproteases are often deliberately used in conjunction with exoproteases to improve these food flavors. Exopeptidases can reduce the amount of peptides with undesirable tastes through the removal of a single hydrophobic amino acid, or pairs of them, from the terminal ends. For example, phenylalanine-containing peptides taste Ͼ100-fold more bitter than does free phenylalanine (13,14). Control and termination of the hydrolytic reaction are therefore crucial for obtaining hydrolysates with the desired organoleptic properties.Enzymes from Aspergillus niger have been used in food production for several decades, and five different endoproteases (PepA to PepE [see reference 26 and references therein]), two carboxypeptidases (CpdI and PepF/CpdII [9, 24, 25]), and one aminopeptidase (ApsA [4]) have been cloned and characterized. Experiments have shown that a particular enzyme preparation of A. niger that contains a specific aminopeptidase activity can liberate phenylalanine from proteins that are present in dough and (semi)hard cheeses (8), thereby improving the flavor and aroma of these products. So far, only one phenylalanine-specific aminopeptidase has been characterized, namely, APF1 from the basidiomycetous fungus Schizophyllum commune (6). APF1 is an intracellular zinc metallo-aminopeptidase that can also hydrolyze an N-terminal tyrosine.In this report, we describe a new aminopeptidase. The gene was cloned from A. niger, and purification and characterization of the gene product show that the gene encodes an aminopeptidase that specifically hydrolyzes amino-terminal phenylalanine and other amino acids with aromatic side groups. ). To study the possible regulation of apsC messenger levels by the carbon and nitrogen source, strain N402 was grown on MM supplemented with either 1% glucose, 1% fructose, and 0.6% NH 4 Cl or 0.4% NaNO 3 or on MM supplemented with 1% bovine serum albumin, 1% elastin, or 1% collagen. RNA was isolated from these cultures and subjected to Northern analysis. MATERIALS AND METHODS StrainsPurification of extracellular ApsC from A. niger NRRL 3112 and peptide sequencing. A. niger NRRL 3112 was grown in a...

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Aminopeptidase C of Aspergillus niger Is a Novel Phenylalanine Aminopeptidase

Basten

Dekker

Schaap

2003

Appl Environ Microbiol

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“…It is reported that A. oryzae has the largest expansion of hydrolytic genes (Vishwanatha et al ., ). Among the proteases secreted by A. oryzae , neutral proteases, the endoproteases involved in elevating utilisation efficiency of proteins during fermentation, are the dominant proteases, whereas acid proteases, the exoproteases involved in FAAs released from proteins and peptides during fermentation, are inadequate (Coenen & Aughton, ; Svendsen & Degan, ; Kitano et al ., ). However , in A. niger , acid proteases were verified as the predominating extracellular proteases, and its maximal proteolytic activity reached 1928 U g −1 during solid fermentation (Gao et al ., ).…”

Section: Introductionmentioning

confidence: 99%

Comparison of physicochemical properties of beef potentiators prepared by synergistic fermentation and traditional method

Gao

Yang

Lü

et al. 2013

Int J of Food Sci Tech

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Beef potentiator was prepared by beef qu, which was previously prepared by a novel synergistic fermentation method (BPSF). Three kinds of other beef potentiators were prepared by commercial enzymes (protamex, flavourzyme and papain, BPCEs), which were used as controls to investigate the physicochemical properties of BPSF. Results showed that BPSF possessed a higher protein recovery (70.99%) and degree of hydrolysis (DH, 51.39%) than BPCEs. The tests of molecular weight distribution and free amino acids (FAAs) indicated that the moderate molecular weight peptides (1-5 kDa) were dominant (70.07-74.43%) in all beef potentiators. The low molecular weight peptides (<1 kDa), umami amino acids and total amino acids in BPSF, were 1.03-to 5.56-, 5.25-to 26.50-and 1.57-to 4.79-fold higher than those in BPCEs, respectively. Meanwhile, hierarchical cluster analysis indicated that BPSF was significantly different to BPCEs, and sensory evaluation showed that BPSF had apparently stronger umami taste than BPCEs.

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“…1992; Svendsen and Degan 1998), have been cloned and characterized. Studies have shown that these enzymes could liberate amino acids from proteins that were present in the dough and cheeses, thereby improving the flavour and aroma of these products (Coenen and Aughton 1998).…”

Section: Introductionmentioning

confidence: 99%

Purification and properties of a novel glycine amino peptidase from Actinomucor elegans and its potential application

Zhou

Yoshimoto

2004

J Appl Microbiol

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X . M A , X . Z H O U A N D T . Y O S H I M O T O . 2004.Aims: To study the properties and show the potential application of a glycine aminopeptidase from Actinomucor elegans. Methods and Results: The enzyme was estimated to have molecular mass of 320 kDa by gel filtration and the subunit size of 56AE5 kDa by SDS-PAGE. It hydrolysed glycine from substrate more efficiently than other amino acids. The optimal temperature for this enzyme was 40°C and at pH 8AE0 it showed its highest activity. The K m and K cat of the enzyme for glycine-b-naphthylamine was 0AE24 mM M and 100AE8 s )1 , respectively. Zinc, copper, cadmium and o-phenanthrolin suppressed almost all enzyme activities at the concentration of 1AE0 mM M. In the process of hydrolysing proteins, it could improve the protease activity considerably.Conclusions: It was a hexamer metalloenzyme which was specific for the substrates with glycinse residue at the N-terminal and some metal cations were needed to maintain its activity. Significance and Impact of the Study: This study demonstrates the properties of a novel aminopeptidase and shows its potential application in the process of the food industry.

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Safety Evaluation of Amino Peptidase Enzyme Preparation derived from Aspergillus niger

Cited by 7 publications

References 7 publications

Aminopeptidase C of Aspergillus niger Is a Novel Phenylalanine Aminopeptidase

Aminopeptidase C of Aspergillus niger Is a Novel Phenylalanine Aminopeptidase

Comparison of physicochemical properties of beef potentiators prepared by synergistic fermentation and traditional method

Purification and properties of a novel glycine amino peptidase from Actinomucor elegans and its potential application

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