Isolation and characterization of an activator-dependent protease from Aspergillus ochraceus screened from low denatured defatted soybean meal and the proteolysis of soy proteins

Zhu, Xiaoxu; Hua, Yufei; Li, Xingfei; Kong, Xiangzhen; Zhang, Caimeng

doi:10.1016/j.lwt.2021.112026

Cited by 6 publications

(7 citation statements)

References 31 publications

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“…Minimally denatured defatted soybean meal (MDSM) is the starting material for the production of a series of soy proteins, such as soy protein isolates and soy protein concentrates. The presence of fungal proteases in fungi‐contaminated MDSM was reported recently 1 . Further studies in our laboratory revealed that more fungi‐originated enzymes were presented in the stored MDSM, including the protease from the fungus of Irpex lacteus , which is a member of the white‐rot fungi and was reported to produce various enzymes, such as peroxidase, beta‐xylanase, glucanase, and cellobiose dehydrogenase 2,3 .…”

Section: Introductionmentioning

confidence: 52%

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Characterization of proteases from Irpex lacteus grown on minimally denatured soybean meal

et al. 2022

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BACKGROUND Acid and thermal stabilities are important properties for the preparation of acidic protein beverage. It is an important method for enzymatic modification to improve the functional properties of protein. Irpex lacteus protease showed a selective hydrolysis to soy proteins. The purpose of this study was to investigate the mechanism of enzymatic hydrolysis and its effects on acid and thermal stabilities of soy proteins. RESULTS The I. lacteus protease selectively hydrolyzed the α and α′ subunits of the native soybean β‐conglycinin (7S globulin) to produce products that presented as the 55 kDa band upon sodium dodecyl sulfate polyacrylamide gel electrophoresis. The amino acid sequences of 55 kDa polypeptides were analyzed in gel multi‐enzyme digestion followed by liquid chromatography–mass spectrometry. By matching the multi‐enzyme digestion peptides with the published polypeptide chain sequences of the α and α′ subunits, it was confirmed that the 55 kDa polypeptides were formed by eliminating amino acid residues on both sides of the N‑ and C‐terminals. From the published protein structure database (https://www.uniprot.org/), it is known that the cleaved peptide bonds were in extension regions. Non‐selective enzyme hydrolysis of both β‐conglycinin (7S globulin) and glycinin (11S globulin), with corresponding drastic increases in the degree of hydrolysis, was observed when the substrates were preheated to the denaturation degree of 40% and above. However, 55 kDa hydrolyzed products and B polypeptides showed some extent of resistance to the proteolysis by I. lacteus protease even if denaturation degree was 100%. Both selective and non‐selective hydrolysis of soy proteins by I. lacteus protease improved the acid and heat stabilities under the same hydrolysis conditions (enzyme/substrate ratio, time, and temperature). CONCLUSION Enzymatic hydrolysis of soybean proteins by the I. lacteus protease can effectively improve the acid and thermal stabilities of proteins. This discovery is significant to avoid aggregation during processing in the beverage industry. In the near future, the protease has potential application value for modification of other proteins. © 2022 Society of Chemical Industry.

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Section: Introductionmentioning

confidence: 52%

“…Our previous study found 28 fungi species in the stored MDSM using rose bengal agar medium 1 . Subsequently, the strains were cultured for a week by transferring to fungi medium separately.…”

Section: Resultsmentioning

confidence: 99%

Characterization of proteases from Irpex lacteus grown on minimally denatured soybean meal

et al. 2022

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“…Effect of compounds such as reducing agents, denaturants, and organic solvents on enzyme activity: According to the method of ZHU [ 46 ] and making appropriate improvements, the reducing agents glutathione (GSH), β-mercaptoethanol, cysteine, denaturant SDS, urea, protease inhibitors PMSF, EDTA, surfactant TritionX-100, and Tween 80, and the organic solvents methanol, ethanol, dimethyl sulfoxide, and ethyl acetate were selected and formulated into appropriate concentrations to determine the effect of each compound on enzyme activity.…”

Section: Methodsmentioning

confidence: 99%

Screening and Characteristics of Marine Bacillus velezensis Z-1 Protease and Its Application of Enzymatic Hydrolysis of Mussels to Prepare Antioxidant Active Substances

et al. 2022

Molecules

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Bacillus velezensis is a type of microorganism that is beneficial to humans and animals. In this work, a protease-producing B. velezensis strain Z-1 was screened from sludge in the sea area near Qingdao (deposit number CGMCC No. 25059). The response surface methodology was used to analyze protease production, and the optimal temperature was 37.09 °C and pH 7.73 with the addition of 0.42% NaCl, resulting in maximum protease production of 17.64 U/mL. The optimum reaction temperature and pH of the protease of strain Z-1 were 60 °C and 9.0, respectively. The protease had good temperature and pH stability, and good stability in solvents such as methanol, ethanol and Tween 80. Ammonium, NH4+,and Mn2+ significantly promoted enzyme activity, while Zn2+ significantly inhibited the enzyme activity. The protease produced by strain Z-1 was used for the enzymolysis of mussel meat. The mussel hydrolysate exhibited good antioxidant function, with a DPPH free radical removal rate of 75.3%, a hydroxyl free radical removal rate of 75.9%, and a superoxide anion removal rate of 84.4%. This study provides a reference for the application of B. velez protease and the diverse processing applications of mussel meat.

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Section: Introductionmentioning

confidence: 99%

“…On the other hand, the adaption of Aspergillus to shifting environments lead to the formation of a particular set of proteins ( Day and Quinn, 2019 ; Wang et al, 2022b ). A. ochraceus has been an important source of industrial enzymes like protease ( El-Khonezy et al, 2021 ; Komarevtsev et al, 2021 ; Zhu et al, 2021 ), esterase ( Romero-Borbón et al, 2018 ) and tannase ( Aracri et al, 2019 ). Several medicinal metabolites, such as an intermediate for the synthesis of desogestrel and eplerenone, are characterized from A. ochraceus ( Wang X. et al, 2020 ; Li et al, 2021 ).…”

Section: Introductionmentioning

confidence: 99%

The Secondary Metabolites and Biosynthetic Diversity From Aspergillus ochraceus

Chen

et al. 2022

Front. Chem.

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Aspergillus ochraceus, generally known as a food spoilage fungus, is the representative species in Aspergillus section Circumdati. A. ochraceus strains are widely distributed in nature, and usually isolated from cereal, coffee, fruit, and beverage. Increasing cases suggest A. ochraceus acts as human and animal pathogens due to producing the mycotoxins. However, in terms of benefits to mankind, A. ochraceus is the potential source of industrial enzymes, and has excellent capability to produce diverse structural products, including polyketides, nonribosomal peptides, diketopiperazine alkaloids, benzodiazepine alkaloids, pyrazines, bis-indolyl benzenoids, nitrobenzoyl sesquiterpenoids, and steroids. This review outlines recent discovery, chemical structure, biosynthetic pathway, and bio-activity of the natural compounds from A. ochraceus.

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Isolation and characterization of an activator-dependent protease from Aspergillus ochraceus screened from low denatured defatted soybean meal and the proteolysis of soy proteins

Cited by 6 publications

References 31 publications

Characterization of proteases from Irpex lacteus grown on minimally denatured soybean meal

Characterization of proteases from Irpex lacteus grown on minimally denatured soybean meal

Screening and Characteristics of Marine Bacillus velezensis Z-1 Protease and Its Application of Enzymatic Hydrolysis of Mussels to Prepare Antioxidant Active Substances

The Secondary Metabolites and Biosynthetic Diversity From Aspergillus ochraceus

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