APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
·
2025
·Vol. 109
·期 1
·1-11
·
IF 4.3
Wang Lihong,Tian Xueqin,Xue Pinghong,Deng Yunhong,Gao Rui,Hu Zhihong
Ergothioneine (EGT) is a rare amino acid with potent antioxidant and anti-inflammatory properties, with a wide range of applications in food, cosmetics, and medicine. In the present study, Aspergillus oryzae , a common edible fungus, was engineered as an optimal host for EGT production. Moreover, two endogenous genes involved in EGT biosynthesis were characterized. The homolog AoEgt1 was shown to be localized in the vacuoles, whereas the homolog AoEgt2 was found in the peroxisomes. Overexpression of EGT biosynthetic genes from different organisms enhanced EGT production, yielding 15.17 mg EGT/g of dry weight. Using glucose as the carbon source and supplementing methionine (Met) as a precursor further increased EGT production to 20.03 mg EGT/g of dry weight, constituting an eight-fold increase compared to the wild-type strain. This study discusses the successful construction of a high-yielding A. oryzae strain for EGT biosynthesis, providing a novel strategy for efficient EGT synthesis. Key points • Two newly described homologs, AoEgt1 and AoEgt2, were identified in A. oryzae. • AoEgt1 and AoEgt2 were found to contribute to EGT biosynthesis. • EGT production was significantly increased by overexpression of Egt1 and Egt2. • Glucose and Met supplementation in the medium increased EGT production.
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FOOD HYDROCOLLOIDS
·
2022
·
IF 11.504
Yan-Wei Liu,Qing-Hao Li,Guo-Qing Huang,Jun-Xia Xiao
The complexation between Aspergillus oryzae lipase (AOL) and chitosan (CS) was investigated as a function of phase separation pH and the resultant complexes were characterized. The results indicated that AOL and CS could assemble micron-sized complexes in pHs 5.0–6.5 and the strongest interaction occurred in pH 5.5. QCM-D analysis revealed that association in pH 5.5 generated a viscoelastic hydrated adlayer with the largest thickness. ITC analysis indicated that the interaction between AOL and CS was driven by enthalpy and the highest one-site binding stoichiometry was recorded in pH 5.5, which was 1.3 and 7.9 times higher than in pHs 5.0 and 6.0, respectively. Both electrostatic attraction and hydrophobic interaction played dominant role in AOL-CS complexation. Compared with free AOL, the interaction with CS reduced its α-helix content, increased its β-sheet content, and changed its tertiary structure; besides, the AOL-CS complex assembled in pH 5.5 exhibited the highest contact angle up to 85.5° and demonstrated enhanced lipase activity retention after incubation in pHs 3.0–9.0 and temperatures 35–75 °C. Hence, the AOL-CS complexes could be used to construct novel biphasic catalysis media based on O/W Pickering emulsions .
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Sustainable Materials and Technologies
·
2021
·
IF 7.053
C.H. Wang,L. Huang,Y. Zhong,X.L. Tong,C.D. Gu,X.H. Xia,Lingjie Zhang,X.L. Wang,J.P. Tu
High-performance lithium ion batteries (LIBs) with high energy/power density are always the persistent pursuit of people. High-quality anode is the key point for the performance improvement of LIBs. In this work, a facile combined strategy is proposed to construct integrated TNO/AOSC electrode, in which Aspergillus Oryzae Spore Carbon (AOSC) conductive matrix is employed to hold Ti 2 Nb 10 O 29 (TNO) nanoparticles . The TNO/AOSC not only shortens electron/ion transfer pathway on account of the nanostructure of TNO, but also provides better chemical stability from AOSC skeleton. Accordingly, the preeminent rate capacity (135.2 mA h g −1 at 10C) and relatively superior cycle stability (a capacity of 149.8 mA h g −1 after 200 cycles at 1C) are obtained for the TNO/AOSC, much better than TNO counterpart. The superior performance of the TNO/AOSC can be ascribed to the beneficial synergistic factors on enhanced electronic conductivity and solider structure from AOSC substrate. This intriguing design strategy may trigger interest for design of other high-quality electrodes in LIBs.
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RSC Advances
·
2019
·Vol. 9
·期 29
·16701-16712
·
IF 3.049
Xiaofeng Li,Maohua Ma,Xuan Xin,Yuqian Tang,Guanglei Zhao,Xinglong Xiao
Gastrodin, a bioactive compound extracted from the plant source of Gastrodia elata Blume, has a wide range of therapeutic effects on central nervous system (CNS) diseases, but suffers from poor brain permeability and short half-life in plasma. In this study, fatty acid esters of gastrodin were successfully synthesized by a whole cell-based biocatalytic method. Aspergillus oryzae cells showed different catalytic activities in the organic solvent systems tested. Tetrahydrofuran was confirmed as the most suitable pure organic solvent, with the highest substrate conversion of 98.0%. Addition of ionic liquids (ILs) into pyridine dramatically accelerated the reaction with conversion increased from 5.9% to 84.2%, and also changed the selectivity of the cells, mainly due to the use of IL-containing systems altering cell permeability and contact of the enzymes with solvent molecules possessing different polarities. The ester products were characterized by 13C-NMR and ESI-MS as gastrodin monoester and diester.
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JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY
·
2016
·Vol. 93
·期 10
·1347-1354
·
IF 1.505
Siyun Gu,Fengqin Feng,Yang Li,Wei Wei,Rongrong Lu
Dioleoyl; palmitoyl-rich triacylglycerols (OPO-rich TAG) were synthesized through Aspergillus oryzae lipase (AOL)-catalyzed acidolysis of palm stearin with commercial oleic acid by a one-step process in a stirred tank reactor and continuous packed bed reactor to evaluate the feasibility of using immobilized AOL. AOL was found to be valuable for the synthesis of OPO-rich TAG when compared with commercial lipase from Thermomyces lanuginose (Lipozyme ® TL IM; Novozymes A/S, Bagsvaerd, Denmark). The C52 (triglycerides with a carbon number of 52, stands for OPO, OPL, LPL and their isomers) content of AOL was higher (45.65 %), and the intensity of treatment (IOT: lipase amount × reaction time/TAG amount) of AOL was just 6.25 % of that of Lipozyme ® TL IM under similar reaction conditions in the stirred tank reactor. Response surface methodology were used to optimize the reaction conditions of the AOL-catalyzed acidolysis is reaction in the packed bed reactor. The optimal point for the set of experimental conditions generated were as follows: residence time 3.0 h; temperature 62.09 °C; substrate molar ratio 7.13 mol/mol. The highest C52 content obtained was 48.60 ± 2.36 %, with 57.46 ± 1.72 % total palmitic acid at the sn -2 position and 74.21 ± 2.45 % oleic acid at the sn -1,3 positions. The half-life of AOL was 24 h in the stirred tank reactor and 140 h in the packed bed reactor. The immobilized AOL achieved similar conversion and selectivity to commercial lipases for the catalyzed synthesis of OPO-rich TAG and may offer a cheaper alternative.
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CHIRALITY
·
2019
·Vol. 32
·期 2
·231-238
·
IF 1.927
Peng Wu,Mengjie Zhang,Yinjun Zhang,Zhao Wang,Jianyong Zheng
In this study, a novel lipase M5 derived from Aspergillus oryzae WZ007 was prone to exhibit high hydrolytic activity and stereoselectivity towards racemic substrate ( R , S )-ethyl 2-bromoisovalerate. ( R )-ethyl 2-bromoisovalerate was obtained by enzymatic resolution, which is the key chiral intermediate for highly efficient enantiomerically fluvalinate. The results showed that the enzymatic reaction was carried out in 120mM racemic substrate for 3 hours, the enantiomeric excess reached 98.6%, the conversion was 51.7%, and E value above 120. Therefore, the novel lipase M5 has the ability to efficiently produce ( R )-ethyl 2-bromoisovalerate, which greatly reduces the industrial production cost of the highly efficient counterpart of fluvalinate.
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JOURNAL OF FOOD SCIENCE
·
2016
·Vol. 81
·期 8
·C1883
·
IF 1.649
Ning Xu,Yaqi Liu,Yong Hu,Mengzhou Zhou,Chao Wang,Dongsheng Li
en The autolyzed mycelia of Aspergillus oryzae are rich in proteins, nucleic acids, sugar, and other biomacromolecules, and are one of the main contributors to the flavor profile of commercially important fermented goods, including soy sauce and miso. We induced autolysis of the mycelia of A. oryzae over 1 to 10 d, and found that the maximum dissolved amounts of total protein and nucleic acid ratio accounted for 28.63% and 88.93%, respectively. The organic acid content, such as citric acid, tartaric acid, succinic acid, lactic acid, and acetic acid, initially increased and then decreased as autolysis progressed, corresponding to changes in pH levels. The main characteristic flavor compounds in soy sauce, namely, ethanol, 2-phenylethanol, and 2-methoxy-4-vinylphenol, were all detected in the autolysate. Subsequently, we tested the effect of adding mycelia of A. oryzae during the fermentation process of soy sauce for 60 d, and found that addition of 1.2‰ A. oryzae mycelia provided the richest flavor. Overall, our findings suggest that compounds found in the autolysate of A. oryzae may promote the flavor compounds of soy sauce, such as alcohols, aldehydes, phenols, and esters. Practical Application pt Autolysate of Aspergillus oryzae mycelium contains rich nutrients and volatile flavor compounds, which is an important component of fermentation seasoning. This study provides a theoretical basis for developing the autolysate products of mycelia of A. oryzae and studying the flavor formation of soy sauce. The autolysate of A. oryzae may also be used to prepare healthy drinks and seasoning products.
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Foods
·
2026
·Vol. 15
·期 10
·1753
·
IF 6
Ting Zhao,Yibing He,Ying Han,Qinhao Liu,Xinqi Jian,Wei Zhao,Chiyue Zhang,Xianbing Xu,Yiying Nian,Zhenyu Wang,Ming Du,Peng Liu,Liming Sun
In our preliminary work, a clam sauce prepared by fermentation withAspergillus oryzae3.042 (AO) exhibited desirable flavor and quality; however, the process was prolonged (exceeding 30 d), and a high salt concentration (6–15%) was necessary to prevent spoilage. Consequently, shortening production cycle and reducing salt content without compromising product quality became a new objective. Enzymatic hydrolysis has long been recognized as an efficient approach in seasoning production, with enzyme efficacy being a key competitive factor. Accordingly, an AO-derived aminopeptidase–protease complex (AOAP) was optimized and prepared as a preparatory step. In this study, AOAP was applied to hydrolyze clam meat to evaluate its potential for producing a seasoning base. A two-step enzymatic hydrolysis process was employed. In the first step, the highest hydrolysis degree (29.1%) was achieved using alkaline protease (AP). The resulting hydrolysate was subsequently subjected to secondary hydrolysis with AOAP, achieving a degree of hydrolysis as high as 49.8%. Sensory evaluation revealed a significant reduction in bitterness and enhancement of umami in the final hydrolysate, a finding corroborated by electronic tongue analysis. Further characterization via LC-MS and amino acid (aa) analysis showed that a substantial number of bitter and umami peptides were released following AP treatment; however, the number of these peptides was markedly reduced after a subsequent AOAP hydrolysis, with concurrent substantial changes in the peptide profile. In the two-step hydrolysate, umami peptides mostly contain 3–10 aa, whereas bitter peptides typically contain only 3–5 aa. The content of free aa increased from 369.17 mg/100 g in the control to 3026.25 mg/100 g in the two-step hydrolysate, half of which were bitter, indicating the debittering efficiency of AOAP. Electronic nose analysis revealed similar flavor profile and characteristic presence of nitrogen oxides in all hydrolysates. GC-MS analysis further demonstrated that, after combined enzymatic hydrolysis, the short-chain aldehydes and ketones responsible for the fishy odor in the raw material almost completely disappeared, while long-chain aldehydes with pleasant aromas were generated. These findings suggest that the secondary hydrolysis step using AOAP can effectively improve the overall flavor profile of the clam hydrolysate, which may support its potential applicability in seasoning production, though further optimization and scale-up validation are needed.
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JOURNAL OF ENVIRONMENTAL MANAGEMENT
·
2022
·
IF 8.91
Kaidi Hu,Jianlong Li,Tianye Zhao,Qiao Zhou,Qin Li,Xinjie Hu,Guoquan Han,Shuhong Li,Likou Zou,Shuliang Liu
As a major intermediate metabolite of synthetic pyrethroids , the occurrence of 3-phenoxybenzoic acid hinders the decomposition of the parent pesticide and poses uncertain risks to environmental ecology and living organisms. Strain Aspergillus oryzae M-4 was previously reported to degrade 3-PBA and several substances were identified as downstream transformation products (TPs). But the mechanism underlying the cleavage of ether bond remains largely unclear. Here, we attempted to address such concern through identifying the peripheral TPs and analyzing transcriptomics, coupled with serial batch degradation experiments. Analysis results of chromatographic/mass spectrometry suggested that 3-PBA underwent twice hydroxylation , to yield mono- and dihydroxylated 3-PBA successively. In parallel, a mutual transformation between 3-PBA and 3-phenoxybenzyl alcohol (3-PBOH) also existed. The proposal of peripheral pathway represents an important advance towards fully understanding the whole 3-PBA metabolism in M-4. A specific altered metabolization was found for the first time, that is, resting cells of M-4 skipped the reduction step and initiate hydroxylation directly, by comparison with growing cells. Transcriptome analysis indicated that 3-PBA induced the up-regulation of genes related to energy investment, oxidative stress response, membrane transport and DNA repair. In-depth functional interpretation of differential expression genes suggested that the generation 3-PBOH and hydroxylated 3-PBA may be due to the participation of flavin-dependent monooxygenases (FMOs) and cytochrome P450 (CYP450), respectively. This study provides new insight to reveal the biodegradation mechanism of 3-PBA by A . oryzae M-4.
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INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY
·
2017
·Vol. 52
·期 12
·2596-2603
·
IF 1.64
Lin Ge,Jingcong Xie,Tao Wu,Shanshan Zhang,Linguo Zhao,Gang Ding,Zhenzhong Wang,Wei Xiao
Summary A novel α-L-rhamnosidase was isolated and purified from Aspergillus oryzae NL-1. The enzyme was purified 13.2-fold by ultrafiltration, ion exchange and gel filtration chromatography with an overall recovery of 6.4% and specific activity of 224.4 U/mg, and the molecular mass of its subunit was approximately 75 kDa. Its optimal temperature and pH were 65 °C and 4.5, respectively. The enzyme was stable in the pH range 3.5–7.0, and it showed good thermostability at higher temperatures. The K M , kcat and kcat/K M values were 5.2 m m , 1624 s −1 and 312 s −1 m m −1 using p NPR as substrates, respectively. Moreover, the enzyme exhibited transglycosylating activity, which could synthesise rhamnosyl mannitol through the reactions of transglycosylation with inexpensive rhamnose as the glycosyl donor. Our findings indicate that the enzyme has potential value for glycoside synthesis in the food industry.
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FOOD CHEMISTRY
·
2024
·
IF 8.5
Chi Zhao,Yuxiang Zhang,Shuangshuang Li,Jiayi Lin,Weifeng Lin,Weixin Li,Lixin Luo
To investigate the mechanism of flavor formation during the traditional preparation Cantonese soy sauce koji (TP), the changes of microorganisms, physicochemical properties, and flavor compounds in TP were comprehensively and dynamically monitored by absolute quantitative methods. Results demonstrated that inoculating Aspergillus oryzae 3.042 in TP was crucial role in enhancing enzyme activity properties. Absolute quantification of flavor combined with multivariate statistical analysis yielded 5 organic acids, 15 amino acids, and 2 volatiles as significantly different flavors of TP. Amplicon sequencing and RT-qPCR revealed that the dominant genera were Staphylococcus , Weissella , Enterobacter , Lactic streptococci , Lactobacillus , and Aspergillus , which exhibited a increasing trend in TP. Correlation analysis exhibited that Staphylococcus and Aspergillus were the pivotal genera contributing to the enzyme activities and flavor of TP. The flavor formation network involved lipid and protein degradation, carbohydrate metabolism and other pathways. Simultaneously, TP can appropriately increase the fermentation time to improve product quality.
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PROTEIN EXPRESSION AND PURIFICATION
·
2018
·
IF 1.338
Jian-yong Zheng,Xing Lan,Xiao-jun Li,Li-juan Huang,Yin-jun Zhang,Zhao Wang
Pichia pastoris expression is a mature and efficient eukaryotic expression system . In this work, Aspergillus oryzae lipase (AOL, with the molecular mass of 28 kDa), which can perform highly stereoselective hydrolysis of (R, S)-methyl 2-(4-hydroxyphenoxy) propanoate, was expressed in P . pastoris X-33. The specific activity of AOL was 432 U/mg, which was obtained by fed-batch cultivation in a 5 L bioreactor using a methanol feeding strategy. After fermentation, the supernatant was concentrated by ultrafiltration with a 10 kDa cut-off membrane and purified with DEAE-Sepharose™ FF ion-exchange chromatography and phenyl Seflnose™ 6 FF hydrophobic interaction chromatography . The purified lipase activity reached 5509 U/mg. AOL showed high activity toward short-chain triacylglyceride (C 4 ), and the optimum temperature and pH were 40 °C and 8.0, respectively. The purified enzyme activity was inhibited by Zn 2+ and Cu 2+ . Moreover, the K m and V max values were 1 mM and 32.89 mmol/min, respectively.
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