Japanese Traditional Miso and Koji Making

Kusumoto, Ken-Ichi; Yamagata, Yuriko; Tazawa, Rina; Kitagawa, M.; Kato, Toshikazu; Isobe, Kenji; Kashiwagi, Yutaka

doi:10.3390/jof7070579

Cited by 47 publications

(27 citation statements)

References 58 publications

(50 reference statements)

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“…The genus Aspergillus belongs to ascomycetes and is a polyphyletic taxon containing many fungi imperfecti [ 34 ]. Generally, Aspergilli are highly capable of decomposing solid polymers and have been widely used in the fermentation industry for a long time [ 35 , 36 ]. Currently, Aspergilli are used as the host microorganisms for production of these compounds owing to their high productivity of proteins and primary and secondary metabolites [ 37 , 38 , 39 , 40 ].…”

Section: Introductionmentioning

confidence: 99%

Aspergillus Hydrophobins: Physicochemical Properties, Biochemical Properties, and Functions in Solid Polymer Degradation

et al. 2022

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Hydrophobins are small amphipathic proteins conserved in filamentous fungi. In this review, the properties and functions of Aspergillus hydrophobins are comprehensively discussed on the basis of recent findings. Multiple Aspergillus hydrophobins have been identified and categorized in conventional class I and two non-conventional classes. Some Aspergillus hydrophobins can be purified in a water phase without organic solvents. Class I hydrophobins of Aspergilli self-assemble to form amphipathic membranes. At the air–liquid interface, RolA of Aspergillus oryzae self-assembles via four stages, and its self-assembled films consist of two layers, a rodlet membrane facing air and rod-like structures facing liquid. The self-assembly depends mainly on hydrophobin conformation and solution pH. Cys4–Cys5 and Cys7–Cys8 loops, disulfide bonds, and conserved Cys residues of RodA-like hydrophobins are necessary for self-assembly at the interface and for adsorption to solid surfaces. AfRodA helps Aspergillus fumigatus to evade recognition by the host immune system. RodA-like hydrophobins recruit cutinases to promote the hydrolysis of aliphatic polyesters. This mechanism appears to be conserved in Aspergillus and other filamentous fungi, and may be beneficial for their growth. Aspergilli produce various small secreted proteins (SSPs) including hydrophobins, hydrophobic surface–binding proteins, and effector proteins. Aspergilli may use a wide variety of SSPs to decompose solid polymers.

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Section: Introductionmentioning

confidence: 99%

Aspergillus Hydrophobins: Physicochemical Properties, Biochemical Properties, and Functions in Solid Polymer Degradation

et al. 2022

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“…Different countries in Asia have different names for their fermented soybean paste, depending on the production process and the type of microbial strain used [5]. In Japan, fermented soybean paste is known as miso [6]; in Korean, doenjang [7]; in China, dajiang [8]; in Thailand, thua-nao [9]; and in Indonesia, tauco [10]. Each product has unique flavor characteristics.…”

Section: Introductionmentioning

confidence: 99%

Nutritional composition of tauco as Indonesian fermented soybean paste

et al. 2022

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Tauco is a fermented soybean paste like miso but typical from Indonesia, commonly used as umami seasoning. This study objective was to evaluate the nutritional composition of diverse tauco products found in Indonesia and to determine a potential tauco product characterized by certain amino acids related to umami peptides (Asp, Glu, Gly, Ser, Thr, Val). Proximate composition, NaCl salt, total sugars, total acids, and total amino acid profiles of 24 tauco products, collected from 24 producers in 7 provinces in Indonesia, were analyzed. The proximate composition mapped tauco into solid (containing 29.2–35.3% moisture on wet weight basis or ww), semisolid (42.2–54.5% ww moisture), and liquid (56.2–68.1% ww moisture). Solid tauco composed of 54.7–65.2% carbohydrates, 10.0–22.8% ashes, 7.13–16.9% NaCl salt, 9.72–11.9% crude proteins, 11.9–27.0% total sugars, 6.98–23.4% crude fats, 1.24–2.18% total acids, and 11.4–17.5% total amino acids on dry weight basis (dw). In contrast, liquid tauco consisted of 8.47–56.5% dw carbohydrates, 17.1–73.8% dw ashes, 10.7–68.4% dw NaCl, 20.4–30.9% dw crude proteins, 4.45–29.9.5% dw total sugars, 1.30–18.9% dw crude fats, 1.65–5.36% dw total acids, and 14.1–24.6% dw total amino acids. All tauco had a slight acidic pH, ranged from 4.38 to 5.91. Glu and Asp were the dominant amino acids of tauco, comprising 25–40% of total amino acids. Mapping of total amino acid profile mentioned a tauco product, characterized by the highest concentration of amino acids related to umami peptides. This finding leads to the exploration of umami peptides to reveal the science behind its traditional use as umami seasoning.

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“…Because bitter-tasting amino acids are generally hydrophobic, it would not be surprising if an abundance of hydrophobic peptides strongly affects the flavors of foods such as still-ripening and well-matured cheeses. As for savory foods, most of them result from protein hydrolysis that occurs in long-cooked foods, fermented foods such as soy, fish, oyster sauces, and miso pastes, and long-matured foods such as cheese and cured meat. − It is now well-accepted that amino acids and peptides contribute significantly to the overall taste of savory foods . While single amino acids are likely to form aroma compounds during thermal and microbiological processing, , peptides may remain more stable and can contribute to taste depending on process parameters.…”

Section: Introductionmentioning

confidence: 99%

Identifying Sequential Residue Patterns in Bitter and Umami Peptides

Dutta

Bereau

Vilgis

2022

ACS Food Sci. Technol.

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A peptide’s amino acid sequence affects its taste, but how? A rigorous structure–property connection is challenging to determine because of both the exponentially growing peptide sequence space and the scarcity of experimental measurements compared to the size of that space. By sensory methods, many peptides have been identified as tasting bitter or umami. Baselines have been determined but relate only single amino acid characteristics, in particular hydrophobicity in bitter peptides and negative charges for umami. In this work, we refine this picture by extracting sequential amino acid patterns. Our method coarse-grains the peptide sequence space to facilitate the systematic identification of common residue patterns. We identify optimal patterns for both bitter and umami peptides: one hydrophobic followed by four polar residues and two negative followed by three polar residues, respectively. We find systematic improvements compared to both random and the baselines mentioned above. Our method complements quantitative structure–activity relationship methods by leveraging sequential information to help locate taste-specific characteristics in peptides and proteins.

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Japanese Traditional Miso and Koji Making

Cited by 47 publications

References 58 publications

Aspergillus Hydrophobins: Physicochemical Properties, Biochemical Properties, and Functions in Solid Polymer Degradation

Aspergillus Hydrophobins: Physicochemical Properties, Biochemical Properties, and Functions in Solid Polymer Degradation

Nutritional composition of tauco as Indonesian fermented soybean paste

Identifying Sequential Residue Patterns in Bitter and Umami Peptides

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