Purification and identification of proteolytic enzymes from Aspergillus oryzae capable of producing the antihypertensive peptide Ile-Pro-Pro

Gotou, Takanobu; Shinoda, Tadashi; Mizuno, Seiichi; Yamamoto, Naoyuki

doi:10.1016/j.jbiosc.2009.01.022

Cited by 21 publications

(22 citation statements)

References 23 publications

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“…Aspergillus oryzae (A. oryzae) is a filamentous fungus listed as a "Generally Recognized as Safe (GRAS)" organism by the US Food and Drug Administration. It has a long history of use in the food industry in the production of traditional fermented foods, due to its high proteolytic activity and its use of sugar [5,6]. According to Machida et al [7] the molecular history of the organism shows that A. oryzae has the largest expansion of hydrolytic genes (135 proteinase genes).…”

Section: Introductionmentioning

confidence: 99%

Protease fromAspergillus oryzae: Biochemical Characterization and Application as a Potential Biocatalyst for Production of Protein Hydrolysates with Antioxidant Activities

Castro

Sato

2014

Journal of Food Processing

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This study reports the biochemical characterization of a protease from Aspergillus oryzae LBA 01 and the study of the antioxidant properties of protein hydrolysates produced with this protease. The biochemical characterization showed that the enzyme was most active over the pH range 5.0–5.5 and was stable from pH 4.5 to 5.5. The optimum temperature range for activity was 55–60°C, and the enzyme was stable at temperatures below 45°C. The activation energy (Ea) for azocasein hydrolysis and temperature quotient (Q10) were found to be 37.98 kJ mol−1 and 1.64–1.53 at temperature range from 30 to 55°C, respectively. The enzyme exhibited t1/2 of 97.63 min and a D value of 324.31 at the optimum temperature for activity (57.2°C). Protease from A. oryzae LBA 01 was shown as a potentially useful biocatalyst for protein hydrolysis, increasing the antioxidant activities of soy protein isolate, bovine whey protein, and egg white protein from 2.0- to 10.0-fold.

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Section: Introductionmentioning

confidence: 99%

Protease fromAspergillus oryzae: Biochemical Characterization and Application as a Potential Biocatalyst for Production of Protein Hydrolysates with Antioxidant Activities

Castro

Sato

2014

Journal of Food Processing

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“…Mizuno, Nishimura, Matsuura, Gotou, and Yamamoto (2004) reported that casein is hydrolyzed by an Aspergillus oryzae protease, Sumizyme FP, and also observed an increased number of proline residues at the second and third positions. Gotou, Shinoda, Mizuno, and Yamamoto (2009) further purified an endopeptidase and an aminopeptidase from Sumizyme FP, which is capable of releasing IPP from β-casein. These two enzymes were identified as neutral protease I (NP I) and leucine aminopeptidase (LAP).…”

Section: Prepared By Other Microbial Enzymesmentioning

confidence: 99%

Preparation, Bioavailability, and Mechanism of Emerging Activities of Ile‐Pro‐Pro and Val‐Pro‐Pro

Zheng

et al. 2019

Comp Rev Food Sci Food Safe

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Ile‐Pro‐Pro and Val‐Pro‐Pro are two most well‐known food‐derived bioactive peptides, initially identified as inhibitors of angiotensin I‐converting enzyme (ACE) from a sample of sour milk. These two peptides were identified in fermented and enzymatic hydrolyzed cow and non‐cow (that is, goat, sheep, buffalo, yak, camel, mare, and donkey) milk, as well as sourdough prepared from wheat, rye, and malt. Similar to other bioactive peptides, bioavailability of these peptides is low (about 0.1%), reaching picomolar concentration in human plasma; they showed blood pressure lowering activity in animals and in human, via improved endothelial function, activation of ACE2, and anti‐inflammatory property. Emerging bioactivities of these two peptides toward against metabolic syndrome and bone‐protection received limited attention, but may open up new applications of these peptides as functional food ingredients. Further studies are warranted to determine the best source as well as to identify novel enzymes (particularly from traditional fermented milk products) to improve the efficiency of production, to characterize possible peptide receptors using a combination of omics technology with molecular methods to understand if these two peptides act as signal‐like molecules, to improve their bioavailability, and to explore new applications based on emerging bioactivities.

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“…Although these tripeptides were not generated from beta-casein via human gastrointestinal enzymes, they were produced in a fermented soybean paste (miso in Japanese) by adding casein (Inoue et al, 2009). Two proteolytic enzymes, which are capable of releasing the tripeptides from casein, were identified in Aspergillus oryzae, one of the starters in fermented foods, such as miso (Gotou et al, 2009).…”

Section: Lactotripeptidesmentioning

confidence: 99%

Drug Discovery Research in Pharmacognosy

Vallisuta¹,

Olimat²

2012

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Purification and identification of proteolytic enzymes from Aspergillus oryzae capable of producing the antihypertensive peptide Ile-Pro-Pro

Cited by 21 publications

References 23 publications

Protease fromAspergillus oryzae: Biochemical Characterization and Application as a Potential Biocatalyst for Production of Protein Hydrolysates with Antioxidant Activities

Protease fromAspergillus oryzae: Biochemical Characterization and Application as a Potential Biocatalyst for Production of Protein Hydrolysates with Antioxidant Activities

Preparation, Bioavailability, and Mechanism of Emerging Activities of Ile‐Pro‐Pro and Val‐Pro‐Pro

Drug Discovery Research in Pharmacognosy

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