Purification and Properties of Leucine Aminopeptidase I from Aspergillus oryzae

Nakadai, Tadanobu; Nasuno, Seiichi; Iguchi, Nobuyoshi

doi:10.1271/bbb1961.37.757

Cited by 35 publications

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“…On the other hand, at pH 4.0 the carboxypeptidase activities of A. oryzae extract were significantly greater than those of A. elegans extract and A. oryzae extract at pH 7.0, especially when the substrates were Z-Glu-Tyr (32.08 μmol/h/mL extract), Z-Leu-Tyr (21.33 μmol/h/mL extract), and Z-Ala-Leu (17.21 μmol/h/mL extract). These observations confirmed that A. oryzae has acidic carboxypeptidases, which is in agreement with earlier reports [17,[33][34][35]. The data presented here indicate that the carboxypeptidase activities in A. oryzae were higher when Tyr and Phe were at the C terminus than when Leu was at the C terminus.…”

Section: Specificity Of a Elegans Carboxypeptidasessupporting

confidence: 93%

Specificity of Carboxypeptidases from Actinomucor elegans and Their Debittering Effect on Soybean Protein Hydrolysates

Yang

2011

Appl Biochem Biotechnol

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The specificities of carboxypeptidases from Actinomucor elegans were investigated by determining enzymatic activities at pH 7.0 and pH 4.0 with 16 Z-dipeptides and three Z-tripeptides as substrates. The debittering effect was evaluated and the free amino acid compositions of the soybean protein hydrolysates were analyzed before and after treatment with A. elegans extract at pH 7.0 and pH 4.0, with carboxypeptidases from Aspergillus oryzae as control. The results of the enzyme activity determinations indicated that carboxypeptidases from A. elegans prefer hydrophobic substrates, such as Z-Phe-Leu, Z-Phe-Tyr-Leu, and Z-Phe-Tyr. The sensory evaluation and free amino acid composition analysis showed that these carboxypeptidases are efficient tools for decreasing the bitterness of peptides because they liberated the fewest free amino acids, which consisted of 73% hydrophobic amino acids, under acidic conditions. Carboxypeptidases from A. elegans display promising prospects for future applications in the protein hydrolysate industry.

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Section: Specificity Of a Elegans Carboxypeptidasessupporting

confidence: 93%

Specificity of Carboxypeptidases from Actinomucor elegans and Their Debittering Effect on Soybean Protein Hydrolysates

Yang

2011

Appl Biochem Biotechnol

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“…A 1200 bp fragment containing the nucleotide sequence of the gene encoding an Aspergillus oryzae/Aspergillus sojae 31 kDa Lap (orLap1) (Nakadai et al, 1973;Chien et al, 2002;US Patent no. 5,994,113) was obtained by PCR of A. oryzae genomic DNA using the oligonucleotides 59-ATGCGTTTCCTCCCCTGCATCGCG-39 (sense) and 59-CAGCGAATCTGCGAAGGCAAGCTC-39 (antisense).…”

Section: Cloning Of Genes Encoding T Rubrum and A Fumigatus Lapsmentioning

confidence: 99%

Aminopeptidases and dipeptidyl-peptidases secreted by the dermatophyte Trichophyton rubrum

et al. 2005

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The nature of secreted aminopeptidases in Trichophyton rubrum was investigated by using a reverse genetic approach. T. rubrum genomic and cDNA libraries were screened with Aspergillus spp. and Saccharomyces cerevisiae aminopeptidase genes as the probes. Two leucine aminopeptidases, ruLap1 and ruLap2, and two dipeptidyl-peptidases, ruDppIV and ruDppV, were characterized and compared to orthologues secreted by Aspergillus fumigatus using a recombinant protein from Pichia pastoris. RuLap1 is a 33 kDa nonglycosylated protein, while ruLap2 is a 58-65 kDa glycoprotein. The hydrolytic activity of ruLap1, ruLap2 and A. fumigatus orthologues showed various preferences for different aminoacyl-7-amido-4-methylcoumarin substrates, and various sensitivities to inhibitors and cations. ruDppIV and ruDppV showed similar activities to A. fumigatus orthologues. In addition to endopeptidases, the four aminopeptidases ruLap1, ruLap2, ruDppIV and ruDppV were produced by T. rubrum in a medium containing keratin as the sole nitrogen source. Synergism between endo-and exopeptidases is likely to be essential for dermatophyte virulence, since these fungi grow only in keratinized tissues.

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“…e e, Cbz-Glu-Tyr; ° 0, Cbz-Glu-Phe; Effect of pH on Acid Carboxypeptidase IV.Peptidase activity was assayed after 20 min incubation at 30'C with four different peptides. 0.05 M CH 3 COONa-HCI buffer ( ) and 0.05 M acetate buffer (---) were used 6. 6, Cbz-Gly-Pro-Leu-Gly; ° 0, Aoc-Gln-LeuGly;.…”

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Purification and Properties of Acid Carboxypeptidase IV fromAspergillus oryzae

Nakadai

Nasuno

Iguchi

1973

Agricultural and Biological Chemistry

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Purification and Properties of Leucine Aminopeptidase I from Aspergillus oryzae

Abstract: An aminopeptidase from Aspergillus orvzae 460 was purified from the rivanol precipitable fraction. The partially purified enzyme was not homogeneous in disc electrophoresis, although symmetric profiles were obtained for enzyme protein and activity in Sephadex gel filtration.

Cited by 35 publications

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Specificity of Carboxypeptidases from Actinomucor elegans and Their Debittering Effect on Soybean Protein Hydrolysates

Specificity of Carboxypeptidases from Actinomucor elegans and Their Debittering Effect on Soybean Protein Hydrolysates

Aminopeptidases and dipeptidyl-peptidases secreted by the dermatophyte Trichophyton rubrum

Purification and Properties of Acid Carboxypeptidase IV fromAspergillus oryzae

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