AoS28D, a proline-Xaa carboxypeptidase secreted by Aspergillus oryzae

Salamin, Karine; Eugster, Philippe J.; Jousson, Olivier; Waridel, Patrice; Grouzmann, Eric; Monod, Michel

doi:10.1007/s00253-017-8186-8

Cited by 9 publications

(3 citation statements)

References 24 publications

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“…There is also a proline-Xaa carboxypeptidase (AoS28D, S28.004) from Aspergillus sp. with different biochemical properties than the other paralogs from gene duplication, which functions together with other secreted aminopeptidases and carboxypeptidases to digest large peptides for uptake [ 112 ].…”

Section: Biological Functions Of Ppcesmentioning

confidence: 99%

Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure, Molecular Properties, and Applications

Baharin

Ting

Goh

2022

Plants

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Proteases or peptidases are hydrolases that catalyze the breakdown of polypeptide chains into smaller peptide subunits. Proteases exist in all life forms, including archaea, bacteria, protozoa, insects, animals, and plants due to their vital functions in cellular processing and regulation. There are several classes of proteases in the MEROPS database based on their catalytic mechanisms. This review focuses on post-proline cleaving enzymes (PPCEs) from different peptidase families, as well as prolyl endoprotease/oligopeptidase (PEP/POP) from the serine peptidase family. To date, most PPCEs studied are of microbial and animal origins. Recently, there have been reports of plant PPCEs. The most common PEP/POP are members of the S9 family that comprise two conserved domains. The substrate-limiting β-propeller domain prevents unwanted digestion, while the α/β hydrolase catalyzes the reaction at the carboxyl-terminal of proline residues. PPCEs display preferences towards the Pro-X bonds for hydrolysis. This level of selectivity is substantial and has benefited the brewing industry, therapeutics for celiac disease by targeting proline-rich substrates, drug targets for human diseases, and proteomics analysis. Protein engineering via mutagenesis has been performed to improve heat resistance, pepsin-resistant capability, specificity, and protein turnover of PPCEs for pharmacological applications. This review aims to synthesize recent structure–function studies of PPCEs from different families of peptidases to provide insights into the molecular mechanism of prolyl cleaving activity. Despite the non-exhaustive list of PPCEs, this is the first comprehensive review to cover the biochemical properties, biological functions, and biotechnological applications of PPCEs from the diverse taxa.

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Section: Biological Functions Of Ppcesmentioning

confidence: 99%

Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure, Molecular Properties, and Applications

Baharin

Ting

Goh

2022

Plants

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“…Their specificities are different and determined by amino acids flanking the proline residue, indicating that they work synergistically. On the other hand, AoS28D is a Pro-Xaa carboxypeptidase that cleaves the C-terminal amino acid when the second C-terminal amino acid is proline [ 51 ]. The serine-type carboxypeptidases discussed above do not have these catalytic activities, but AoS28D can release Xaa from -Pro-Xaa at pH 3.8 and 7.0 and also Xaa-amide from -Pro-Xaa-amide.…”

Section: Koji Enzymes Involved In Miso Makingmentioning

confidence: 99%

Japanese Traditional Miso and Koji Making

Kusumoto

Yamagata

Tazawa³

et al. 2021

JoF

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Miso is a traditional Japanese seasoning paste produced by fermenting soybeans using the power of koji mold. A recent Japanese cohort study has shown that increased consumption of fermented soybean products is associated with a reduced risk of death in both men and women. In this review, we briefly explain what miso means in the Japanese culture and food industry, varieties of miso available today, and steps involved in miso making. Then, we review early and latest scientific researches in koji mold species, their safety, and beneficial enzymes they produce during fermentation and maturation processes, which play a major part in determining the quality and sensory profile of miso.

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“…The TEPs currently used in the food industry are derived mainly from microorganisms, such as Aspergillus spp. [6][7][8][9] and Bacillus spp. [10][11][12][13].…”

Section: Introductionmentioning

confidence: 99%

A fast and novel approach to evaluate technical enzyme preparations for an efficient protein hydrolysis

Großmann

Merz

Appel

et al. 2019

Eur Food Res Technol

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The objective of this study was to establish a fast approach (< 1 h) for the evaluation of technical enzyme preparations (TEPs). An automated photometric analyzer (Gallery TM Plus) was equipped with 32 synthetic and natural substrates to measure aminopeptidase, carboxypeptidase, dipeptidyl peptidase and endopeptidase activities distinguishably and the proteolytic activity towards lupine protein of TEPs. The established so-called "activity fingerprints" (AFPs) delivered detailed information about the substrate spectra and peptidase side activities, noticing furthermore batch variations of Flavourzyme1000L. Based on their AFPs, particular TEPs were selected for lupine protein hydrolysis and the hydrolysates were analyzed regarding the degree of hydrolysis and the free amino acids. It was demonstrated that the information of the AFPs were applicable to predict important properties of the resulting hydrolysates. Consequently, the hydrolysis efficiency was improved (increase of 47%). The system introduced enables the targeted selection of TEPs for enzymatic protein hydrolysis, resulting in specific food protein hydrolysates. Keywords Technical enzyme preparation • Peptidase activity • Substrate screening • Protein hydrolysis • Targeted hydrolysate attribute Abbreviations Alc Alcalase2.4L AFP Activity fingerprint BEH Ethylene bridged hybrid CAGR Compound annual growth rate CV Coefficients of variation DPP Dipeptidyl peptidase DH Degree of hydrolysis DZM DeltazymAPS-M-FG FP51 FoodPro51FP FVZ Flavourzyme1000L H 2 O dd Purified water h Concentration of free amino groups h tot Maximum concentration of free amino acids at complete hydrolysis LAPU Leucine aminopeptidase units LOD Limit of detection LOQ Limit of quantification OPA ortho-Phthalaldehyde P278 Promod278 PepR PeptidaseR pNA para-Nitroaniline TEP Technical enzyme preparation UPLC Ultra-performance liquid chromatography Electronic supplementary material The online version of this article (

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AoS28D, a proline-Xaa carboxypeptidase secreted by Aspergillus oryzae

Cited by 9 publications

References 24 publications

Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure, Molecular Properties, and Applications

Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure, Molecular Properties, and Applications

Japanese Traditional Miso and Koji Making

A fast and novel approach to evaluate technical enzyme preparations for an efficient protein hydrolysis

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