JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
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2013
·
IF 2.823
Jian-Yong Zheng,Jia-Yu Wu,Yin-Jun Zhang,Zhao Wang
The mycelium of Aspergillus oryzae WZ007 was successfully developed to kinetic resolution of ( R , S )-ethyl-2-(4-hydroxyphenoxy) propanoate (( R , S )-EHPP) for production of ( R )-ethyl-2-(4-hydroxyphenoxy) propanoate (( R )-EHPP). The key biocatalytic process parameters (pH, temperature, rotation speed and substrate concentration) were optimized. Under the optimum conditions, the optical purity of ( R )-EHPP was improved up to >99% when the conversion was above 49%. A. oryzae WZ007 whole-cell lipase exhibited high reaction capacity, enantioselectivity and good reusability. The tolerable substrate concentration was 0.5 mol/L, and dry mycelium of A. oryzae WZ007 maintains over 80% of its initial activity after eight repeating cycles. Therefore the enzymatic preparation of ( R )-EHPP route was suitable for industrial application.
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Frontiers in Microbiology
·
2023
·
IF 5.2
Li Heng,Lu Zhen-Ming,Deng Wei-Qin,Zhang Qi-Sheng,Chen Gong,Li Qi,Xu Zheng-Hong,Ma Yan-He
Broad bean paste-meju was fermented by a mixture of broad bean koji and saline; koji fermentation is an essential process for the production of broad bean paste-meju. Aspergillus oryzae was the most widely used in sauce fermentation. The purpose of this study was to research the factory adaptability of the highly efficient A. oryzae PNM003 and further evaluate the effect of fermentation conditions and fermentation strains on koji. A. oryzae PNM003 was compared with the widely used strain HN 3.042 not only in the laboratory but also in factory conditions (large scale). Results showed that the koji made with the same starter in the factory had a greater amount of fungi than that in the laboratory. Bacteria and yeast levels in HN_L koji were higher than in PN_L koji. As for fungi constitution, almost only Aspergillus survived in the end through the microorganism self-purification process during koji fermentation. As for the bacterial constitution, koji was grouped by fermentation conditions instead of fermentation starter. PN koji had higher protease activity and a higher content of total acids, amino acid nitrogen, amino acids, and organic acids in the laboratory conditions. Nevertheless, in factory conditions, PN koji and HN koji had similar indexes. As for volatile flavor compounds, koji made with the two starters in the same condition was grouped together. As for the same starter, there were more flavor compounds metabolized in the factory condition than in the laboratory condition, especially esters and alcohols. The results showed PN was a highly efficient strain to ferment koji, but the advantages were expressed more remarkably in laboratory conditions. In brief, the fermented condition had a greater influence than the fermentation starter for broad bean koji.
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Frontiers in Molecular Biosciences
·
2021
·
IF 5.246
Qu Tianle,Zhang Chunyue,Qin Zhen,Fan Liqiang,Jiang Lihua,Zhao Liming
Aminooligosaccharides possess various biological activities and can exploit wide applications in food, pharmaceutical and cosmetic industries. Commercial aminooligosaccharides are often prepared by the hydrolysis of chitin and chitosan. In this study, a novel GH family 20 β-N-acetylhexosaminidases gene named AoNagase was cloned from Aspergillus oryzae and expressed in Pichia pastoris. The purified AoNagase had maximal activity at pH 5.5 and 65°C. It exhibited good pH stability in the range of pH 6.0–7.5 and at temperatures below 50°C. AoNagase was capable of hydrolyzing not only colloidal chitosan (508.26 U/mg) but also chitin (29.78 U/mg). The kinetic parameters (Km and Vmax) of AoNagase were 1.51 mM, 1106.02 U/mg for chitosan and 0.41 mM, 40.31 U/mg for colloidal chitin. To our knowledge, AoNagase is the first GH family 20 β-N-acetylhexosaminidase capable of hydrolyzing both chitosan and chitin. AoNagase is an endo-type β-N-acetylhexosaminidases and can potentially be used for the manufacturing of aminooligosaccharides.
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JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
·
2020
·
IF 4.192
Xianli Gao,Ermeng Liu,Yiyun Yin,Lixin Yang,Qingrong Huang,Sui Chen,Chi-Tang Ho
Aspergillus oryzae 3.042 was mutagenized using atmospheric and room-temperature plasma (ARTP) technology to enhance its salt-tolerant proteases activity. Compared to the starting strain, mutant H8 subjected to 180 s of ARTP treatment exhibited excellent genetic stability (15 generations), growth rate, and significantly increased activities of neutral proteases, alkaline proteases, and aspartyl aminopeptidase during fermentation. Mutant H8 significantly enhanced the contents of 1–5 kDa peptides, aspartic acid, serine, threonine, and cysteine in soy sauce by 16.61, 7.69, 17.30, 8.61, and 45.00%, respectively, but it had no effects on the contents of the other 14 free amino acids (FAAs) due to its slightly enhanced acidic proteases activity. Analyses of transcriptional expressions of salt-tolerant alkaline protease gene (AP, gi: 217809) and aspartyl aminopeptidase gene (AAP, gi: 6165646) indicated that their expression levels were increased by approximately 30 and 27%, respectively. But no mutation was found in the sequences of AP and AAP expression cassettes, suggesting that the increased activities of proteases in mutant H8 should be partially attributed to the increased expression of proteases. ARTP technology showed great potential in enhancing the activities of salt-tolerant proteases from A. oryzae.
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RENEWABLE ENERGY
·
2024
·
IF 9
Shuaibo Xia,Cai Shen,Jiale Lin,Maolin Tu,Chin-Ping Tan,Ling-Zhi Cheong
The absorption process of Aspergillus oryzae lipase (AOL) onto the surface of ZIF-8 was elucidated using molecular dynamic (MD) simulation. AOL are absorbed onto the surface of ZIF-8 via hydrogen bonding, electrostatic and van der Waals interaction with minimal changes to its native configurations. Unlike free AOL, AOL@ZIF-8 can maintain its structure in simulated methanol solutions. To verify the results from MD simulation, AOL was immobilized onto ZIF-8 (AOL@ZIF-8: immobilization efficiency of 64.71 % and a protein loading of 57.36 mg/g) and characterized using SEM, FTIR, and XRD. As compared to free AOL, AOL@ZIF-8 demonstrated higher transesterification activity with an activity recovery of 106.18 %. In agreement with MD simulations, AOL@ZIF-8 exhibited enhanced stability in wide range of pH and under presence of alcohol solution. AOL@ZIF-8 can be used to catalyze transesterification of used cooking oil for production of biodiesel (FAME content of 81.19 %).
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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2023
·
IF 8.2
Yan-Wei Liu,Qing-Hao Li,Shi-Yu Li,Guo-Qing Huang,Jun-Xia Xiao
To prompt the application of the chitosan (CS)- Aspergillus oryzae lipase (AOL) complex in the construction of novel biphasic catalysis medium, its Pickering emulsion stabilization ability as well as adsorption behavior in the oil-water interface were investigated and the stability of resultant emulsion was evaluated. The results indicated that the CS-AOL complex assembled in mass ratio 1:5 was an effective Pickering stabilizer and up to 90 % AOL could be retained in the emulsion interface. Quartz crystal microbalance with dissipation monitoring suggested that the CS-AOL complex spontaneously absorbed to oil-water interface; absorption dynamics analysis revealed that the adsorption was driven by diffusion accompanied by rapid structural rearrangement; while interfacial dilatational rheology demonstrated the formation of an elastic film in the oil-water interface. The Pickering emulsions were pseudoplastic and that in oil fraction 0.6 exhibited the elastic behavior in contrast to the viscous behavior in oil fractions 0.2 and 0.4. The Pickering emulsion exhibited excellent stability against storage for up to 28 d, pHs 2.0–12.0, heating at 25–90 °C, and up to 500 mmol/L NaCl, and the corresponding interfacial AOL retentions exceeded 80 % during exposure to these conditions. Hence, the CS-AOL complex could be used as a stabilizer to construct Pickering emulsion-based biphasic catalysis systems.
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Food Bioscience
·
2024
·
IF 4.8
Hua-Wei Zhang,Ke Cheng,Jing-Jing Tang,Ling-Zhi Liu,Ruo-Xuan Qin,Yi-Nuo Sun,Jiang-Hua Zhang,Da-Yong Zhou
To synthesize structured phospholipids (SPLs) in an efficient and green manner is of great significance. Herein, novel Fe 3 O 4 @SiO 2 - Aspergillus oryzae lipase (AOL)/copper phosphate trihydrate nanoflowers (FLCNs) were prepared by coprecipitation method and then characterized by energy-dispersive X-ray spectroscopy, X-ray photoelectron spectroscopy, Fourier transform infrared spectroscopy, and vibrating sample magnetometer etc. FLCN activity was further evaluated by promoting functional medium-chain SPL (MCSPL) or short-chain SPL (SCSPL) synthesis via biotransesterification between soybean lecithins and medium-chain fatty acids (MCFAs) or short-chain fatty acids (SCFAs) under optimal reaction conditions. Moreover, FLCNs and free AOLs were comparatively assayed in enzymatic properties. As a result, FLCNs were successfully fabricated with sufficiently large surfaces and numerous enzyme active sites. Owing to these structural features, after reacting at 40 °C for 36 h with FLCN dosage of 6% and substrate mass ratio of 1:3:3, FLCNs exhibited much more excellent activity in MCSPL synthesis with 88.30 ± 0.63% of MCFA incorporation than benchmark enzymes and heterogeneous functional materials. Most significantly, in the first biosynthesis of functional SCSPLs facilitated by FLCNs, much superior SCFA incorporation of 66.55 ± 0.73% was obtained. Notably, FLCNs also possessed convenient magnetic separability together with superior pH and temperature tolerances, thermal and storage stabilities, and recyclability to free AOLs. In brief, the present investigation provides a new biological strategy for effective, economic, convenient, and eco-friendly SPL synthesis in food and pharmaceutical industries, highlighting its merits in functional lipid production.
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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2024
·
IF 7.7
Palanisamy Vasudhevan,Dharman Kalaimurugan,Sivarasan Ganesan,Naveed Akbar,Saurav Dixit,Shengyan Pu
Agricultural residues are one of the most cost-effective and readily accessible carbon resources for producing commercially significant enzymes. Several enzymes have been used in different industries like pharmaceuticals, foods, textiles, and dyes that can be generated by various species of microbes found in waste from agriculture. The current research investigated laccase production by Aspergillus oryzae utilizing agricultural wastes. Physical and chemical properties, including pH, temperature, sucrose, yeast extract, and copper sulfate levels, were optimized. The utilization of the response surface methodology along with the centralized composite design method, which assesses multiple media parameters and utilizes a two-level experimental approach, aids in determining the variable and its significance in increasing production quality. The centralized composite design enhancement showed that the optimal conditions for highest laccase activity (623.16 U/mL) were pH 7.0, temperature 25 °C, corn cobs as substrate, sucrose (2.0 %), yeast extract (1.0 %), and copper sulfate (0.1 mM) level. The laccase enzyme was optimized using various pH, temperature, metal ions, and inhibitors combinations. The extracted laccase enzyme maximum activity was attained at pH 6.0 and 40 °C. The inclusion of divalent ions can enhance laccase activity, while the use of various inhibitors decreases laccase activity. Under various pH circumstances, the Aspergillus oryzae laccase enzyme can successfully degrade p-chlorophenol. The present study describes statistically validated optimal methodologies for enhancing laccase synthesis, leading to a laccase production technique that is simultaneously highly efficient and economically profitable, with possible use of p-chlorophenol degradation.
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CATALYSIS COMMUNICATIONS
·
2013
·
IF 2.915
Hong-De Yan,Qun Zhang,Zhao Wang
A lipase from Aspergillus oryzae WZ007 exhibited high esterification activities toward a series of short-chain acids and alcohols. Moreover, it displayed a strong tolerance for high substrate concentration of up to 2.0 M and presented a highest initial rate of 276 mmol·L − 1 ·h − 1 at this concentration. After a reaction time of 48 h, the conversion rates of acids were higher than 80% for the synthesis of a majority of heptanoic acid esters, some octanoic acid esters and n -propyl hexanoate. These results implied that A. oryzae WZ007 lipase was a promising biocatalyst in the production of flavor esters.
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BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY
·
2016
·Vol. 64
·期 2
·251-258
·
IF 1.429
Hong-De Yan,Zhao Wang,Jun-Qing Qian
A mycelium-bound lipase from Aspergillus oryzae (AOL) exhibited excellent enantioselectivity for kinetic resolution of ( RS )-1-phenylethanol (( RS )-1-PE) in organic solvent. The various reaction parameters affecting the conversion and enantioselectivity were studied, including type of acyl donor, solvent, molar ratio, temperature, enzyme amount, and substrate concentration. The optimum reaction conditions were found to be transesterification with vinyl acetate at 30 °C in methyl tert -butyl ether with a vinyl acetate: ( RS )-1-PE molar ratio of 1:1 and an enzyme concentration of 60 g/L. At the optimum reaction conditions, the conversion could reach above 46% with >99% enantiomeric excess of the product, ( R )-1-phenylethyl acetate, when the substrate concentration was below 1.4 M. The enzyme displayed an excellent enantioselectivity with an E -value of >200 and a strong tolerance for high substrate concentration of up to 1.8 M. Those results indicated that AOL was a promising biocatalyst in the kinetic resolution of ( RS )-1-PE.
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Biomolecules
·
2025
·Vol. 15
·期 12
·1695
·
IF 4.8
Desheng Wu,Maohua Ma,Xiaohan Liu,Xiaofeng Li,Guanglei Zhao
Propionylated derivatives of gastrodin are valuable due to their enhanced lipophilicity and bioavailability. This study investigated the molecular basis for the differential catalytic efficiency ofAspergillus oryzaewhole cells in gastrodin propionylation. A high conversion rate of 96.84% was achieved with soybean oil induction, compared to only 8.23% under glucose induction. Comparative transcriptomic analysis identified 20,342 differentially expressed genes (DEGs), which were significantly enriched in lipid metabolism and signal transduction pathways. From 26 upregulated lipase-related DEGs, a candidate triacylglycerol lipase gene (CL24.Contig40_All) was prioritized. Homology modeling and molecular docking supported its potential role by demonstrating that the encoded enzyme possesses a typical α/β hydrolase fold with a catalytic triad and favorable binding with both gastrodin and vinyl propionate. These findings indicate that soybean oil may enhance lipase expression by activating lipid metabolic and phosphatidylinositol signaling pathways, providing crucial transcriptional-level insights and genetic targets for the rational design of efficient whole-cell biocatalysts.
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APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
·
2024
·
IF 3.1
Zhang Yueting,Nie Hongmei,Zhang Fei,Jin Mengmeng,Wang Zhao,Zheng Jianyong
Aspergillus oryzae is an ideal cell factory for protein expression with powerful protein processing and secretion capabilities. The current study aimed to explore the homologous expression of A. oryzae lipase AOL (GenBank: KP975533) by constructing an auxotrophic A. oryzae △ pyrG △ nptB and subsequently characterizing the immobilization and catalytic properties of recombinant lipase. Initially, the pyrG gene knocked out in wild-type A. oryzae by homologous recombination, followed by the creation of a uridine/uracil auxotroph transformation. Through this system, the protease gene nptB was precisely knocked out, leading to a substantial decrease in extracellular (39.04%) and intracellular (90.07%) protease activity. The A. oryzae △ nptB △ pyrG strain was used as host for homologous expression of lipase AOL. After transformation of linearized lipase-expression cassette, the engineered A. oryzae AOL-8 was screened out with the lipase gene copy number of 14, exhibiting extracellular and intracellular lipase activities of 1.75 U/mL and 46.4 U/g, respectively. Subsequently, the production and immobilization of the recombinant lipase, via physical adsorption on macroporous resin XRZ04B, were achieved through submerged fermentation of the AOL-8 strain. The results of esterification catalytic properties of immobilized recombinant lipase indicated that the lipase exhibited optimal catalytic activity with lauric acid and methanol as substrates, a reaction temperature of 35 °C, and n-hexane as the preferred solvent medium; its highest conversion rate can reach at 72.3%.
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