Purification, characterisation and salt-tolerance molecular mechanisms of aspartyl aminopeptidase from Aspergillus oryzae 3.042

Gao, Xianli; Yin, Yiyun; Zhou, Cunshan

doi:10.1016/j.foodchem.2017.07.081

Cited by 31 publications

(29 citation statements)

References 34 publications

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“…Molecular weight of the isolated AP was determined using 10% SDS‐PAGE gel . NP I was isolated in light of the method described in our previous work . The prepared sample was placed at 4 °C for further analyses using matrix‐assisted laser desorption ionization time‐of‐flight/time‐of‐flight mass spectrometry (MALDI‐TOF/TOF‐MS).…”

Section: Methodsmentioning

confidence: 99%

“…Crude protease extraction from A. oryzae 3.042 koji A. oryzae 3.042 was cultured according to a method described previously. 8 Proteases were extracted from 15 g of pulverized koji (10 s) using 100 mL of sodium phosphate buffer (100 mmol L −1 , pH 6.0) with 1 mmol L −1 phenylmethylsulfonyl fluoride (PMSF) and 2 mmol L −1 calcium acetate (buffer A) in a rotary shaker (200 rpm) at 4 ∘ C for 1 h. The fungal mycelia and medium debris were removed from the obtained extract by centrifugation at 5000 × g (4 ∘ C, 15 min). The resulting supernatant was saturated to 30% by slowly adding solid ammonium sulfate in an ice-water bath stirring with a magnetic bar (200 rpm).…”

Section: Protease Activity Assaymentioning

confidence: 99%

“…Previous studies demonstrated that alkaline protease (AP), the most abundant protease secreted by A. oryzae , was highly associated with the quality of soy sauce and the utilization rate of raw materials . Unfortunately, the current quality of soy sauce and the utilization rate of raw materials in China are still low, leading to their weak competitiveness in both foreign and domestic markets . APs from other strains, such as Bacterium sp., Bacillus subtilis , Streptomyces clavuligerus and A. oryzae , were found to be salt‐tolerant.…”

Section: Introductionmentioning

confidence: 99%

“…Recently, many protein tertiary structures have been determined by X‐ray crystallography and NMR spectroscopy, leading to bioinformatics tools more powerful and reliable for analyzing the structures of biomacromolecules . In a previous study, we successfully employed the SWISS‐MODEL program to model the three‐dimensional structure, the NAMD and VMD to perform molecular dynamics (MD), and the PredictProtein server programs to calculate the secondary structure, solvent accessibility and the interior hydrophobicity of aspartyl aminopeptidase from A. oryzae 3.042 . Here, we aim to elucidate the biochemical properties and salt‐tolerant mechanisms of AP using a non‐salt‐tolerant neutral protease I (NP I) as control, which was also previously isolated from A. oryzae 3.042.…”

Section: Introductionmentioning

confidence: 99%

“…6,7 Unfortunately, the current quality of soy sauce and the utilization rate of raw materials in China are still low, leading to their weak competitiveness in both foreign and domestic markets. 8 APs from other strains, such as Bacterium sp., 9 Bacillus subtilis, 10 Streptomyces clavuligerus 11 and A. oryzae, 12 were found to be salt-tolerant. However, to date, comparatively little has been revealed about the biochemical properties and salt-tolerant mechanisms of AP produced from A. oryzae 3.042.…”

Section: Introductionmentioning

confidence: 99%

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Separation, biochemical characterization and salt‐tolerant mechanisms of alkaline protease from Aspergillus oryzae

et al. 2019

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BACKGROUND The salt tolerance of proteases secreted by Aspergillus oryzae 3.042 closely relates to the utilization of raw materials and the quality of soy sauce. However, little is known about the salt‐tolerant proteases and their salt‐tolerant mechanisms. RESULTS In this study, we isolated and identified a salt‐tolerant alkaline protease (AP, approximately 29 kDa) produced by A. oryzae 3.042. It was considered as a metal‐ion‐independent serine protease. The optimum and stable pH values were both pH 9.0 and the optimum temperature was 40 °C. Over 20% relative activity of AP remained in the presence of 3.0 mol L−1 NaCl after 7 days, but its Km and Vmax were only mildly influenced by the presence of 3.0 mol L−1 NaCl, indicating its outstanding salt tolerance. Furthermore, AP was more stable than non‐salt‐tolerant protease at high salinity. The salt‐tolerant mechanisms of AP could be due to more salt bridges, higher proportion of ordered secondary structures and stronger hydrophobic amino acid residues in the interior. CONCLUSIONS The above results are vital for maintaining, activating and/or modulating the activity of AP in high‐salt environments. They would also provide theoretical guidance for the modification of AP and the engineering of A. oryzae 3.042 so as to secrete more AP. © 2018 Society of Chemical Industry

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Section: Methodsmentioning

confidence: 99%

Section: Protease Activity Assaymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Separation, biochemical characterization and salt‐tolerant mechanisms of alkaline protease from Aspergillus oryzae

et al. 2019

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Therapeutic and biotechnological applications of substrate specific microbial aminopeptidases

Nandan

Nampoothiri

2020

Appl Microbiol Biotechnol

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Aminopeptidases (EC 3.4.11.) belongs to exoprotease family, which can catalyze the cleavage of peptide bond which connects the N-terminal amino acid to the penultimate residue in a protein. Aminopeptidases catalyze the process of removal of the Nterminal amino acids of target substrates by sequential cleavage of one amino acid residue at a time. Microbial aminopeptidase are of great acceptance as industrial enzymes with varying applications in food and pharma industry since these enzymes possess unique characteristics than aminopeptidases from other sources. This review describes the various applications of microbial aminopeptidases in different industrial sectors. These enzymes are widely used in food industry as a debittering agent as well as in the preparation of protein hydrolysates. In baking, brewing, and cheese making aminopeptidases are extensively used for removing the bitterness of peptides. The inhibitors of these enzymes are found great clinical applications against various diseases such as cancer, diabetes, and viral infections. Aminopeptidases are widely used for the synthesis of biopeptides and amino acids, and found to be efficient than chemical synthesis. These enzymes are capable of hydrolyzing organophosphate compounds, thus having biological as well as environmental significance. Key Points• Cleaves the amino-terminal amino acid residues from proteins and peptides.• Microbial aminopeptidase are of great acceptance as both therapeutic and industrial enzyme.• Review describes the potential applications of microbial aminopeptidases.

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From bitter to delicious: properties and uses of microbial aminopeptidases

Wang

Zhao

Zhao³

et al. 2023

World J Microbiol Biotechnol

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Purification, characterisation and salt-tolerance molecular mechanisms of aspartyl aminopeptidase from Aspergillus oryzae 3.042

Cited by 31 publications

References 34 publications

Separation, biochemical characterization and salt‐tolerant mechanisms of alkaline protease from Aspergillus oryzae

Separation, biochemical characterization and salt‐tolerant mechanisms of alkaline protease from Aspergillus oryzae

Therapeutic and biotechnological applications of substrate specific microbial aminopeptidases

From bitter to delicious: properties and uses of microbial aminopeptidases

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