Biomolecules
·
2025
·Vol. 15
·期 12
·1695
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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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3 Biotech
·
2019
·Vol. 9
·期 7
·1-9
·
IF 1.786
Yan Hong De,Guo Bing Han,Wang Zhao,Qian Jun Qing
The lipase from Aspergillus oryzae was modified with a surfactant and then observed to exhibit high catalytic efficiency and enantioselectivity for the kinetic resolution of ( RS )-1-phenylethanol. The influential factors of the modified-lipase preparation were investigated, including the surfactant source, the organic cosolvent, and the buffer pH. The optimum modification conditions were found with a surfactant of polyoxyethylene sorbitan monopalmitate, an organic cosolvent of tetrahydrofuran and a phosphate buffer of pH 7.0. In the transesterification of ( RS )-1-phenylethanol with vinyl acetate, the surfactant-modified lipase showed excellent enantioselectivity for the R -isomer ( E > 200), giving an enantiomeric excess of higher than 99% for ( R )-1-phenylethyl acetate at 46.8% conversion with the reaction time of 2 h at 30 °C. The enzymatic activity had barely altered after 30 days even at 50 °C when it was saved in a powdered state. The results indicated that the modification strategy was useful and highly efficient, and that modified A. oryzae lipase was a promising biocatalyst in the kinetic resolution of ( RS )-1-phenylethanol.
研究领域:
生物化学
·
酶工程
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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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Food Bioscience
·
2022
·
IF 5.318
Chengtuo Niu,Xianlei Xing,Xiaohong Yang,Feiyun Zheng,Chunfeng Liu,Jinjing Wang,Qi Li
This study aimed to obtain an Aspergillus oryzae strain with high protease activity and to evaluate its potential to apply as starter culture in bean-based fermented foods (BBFFs) production using doubanjiang fermentation as research model. A. oryzae BL18 with higher protease activity than the commonly used starter A. oryzae 3.042 was obtained through two rounds of screening. Moreover, this strain was also proved to be safe to apply in BBFFs fermentation due to the lack of the ability to produce aflatoxin B1 through genomic and experimental analysis. A. oryzae BL18 was optimal to grow under 0–12% salinity, 25–40 °C and pH4-6. During koji -making, A. oryzae BL18 had stronger ability to produce spores (4.19 × 10 8 spores/g dry weight) and to secrete protease (4654.35 U/g) than A. oryzae 3.042 (2.89 × 10 8 spores/g dry weight and 3604.40 U/g). Significantly higher concentrations of umami amino acids and volatile flavor compounds were found in doubanjiang fermentation inoculated by A. oryzae BL18 while better sensory characteristics were observed. Therefore, A. oryzae BL18 might be a promising starter to apply in fermentation of doubanjiang or other BBFFs.
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LWT-FOOD SCIENCE AND TECHNOLOGY
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2022
·
IF 6.056
Chunyun Ma,Yan Zhang,Chuankai Yang,Yuhang Zhang,Miaorong Zhang,Jianguo Tang
Cetyl trimethyl ammonium bromide (CTAB)-activated lipase-mineral hybrid microflowers (CTAB-Lip-MHFs) were fabricated via biomineralization using Cu 3 (PO 4 ) 2 ⋅3H 2 O as the mineral for olive oil hydrolysis. FT-IR spectra indicated that immobilized lipase molecules in CTAB-Lip-MHFs has good structural integrity, and XPS spectra revealed that immobilized lipase molecules were present at the surface of CTAB-Lip-MHFs. Kinetic studies suggested that CTAB-Lip-MHFs had good substrate affinity ascribed to interfacial effect caused by CTAB, meanwhile, the open conformation of lipase activated by CTAB contributed to increased reaction rate with substrate. The generated fatty acids via hydrolysis of olive oil by CTAB-Lip-MHFs were 146% of that by free lipase, moreover, CTAB-Lip-MHFs could retain 76.5% and 93.2% of initial activities after storage at 50 °C for 10 h and 4 °C for 30 days, respectively, indicating the good stability of CTAB-Lip-MHFs. In addition, after 5 recycles, CTAB-Lip-MHFs preserved 72.7% of initial activity, demonstrating the favorable reusability of CTAB-Lip-MHFs for fatty acid production.
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PROCESS BIOCHEMISTRY
·
2022
·
IF 4.885
Han Wei,Qian Wang,Rongjing Zhang,Maogen Liu,Weiwei Zhang
To achieve an efficient and cost-effective conversion from waste cooking oil (WCO) to biodiesel, a facile one-pot co-immobilization of Aspergillus oryzae lipase (AOL) and Rhizomucor miehei lipase (RML) was developed by rapid encapsulation of magnetic chitosan microcapsules. The encapsulation process was accomplished by self-assembly of negatively charged magnetic nanoparticles (citrate modified Fe 3 O 4 ) on ionic cross-linked chitosan-citrate aggregates containing lipases. Integrating Tween 80 bio-imprinting of lipases, the co-immobilized AOL@RML (co-im Tween 80-AOL@RML) achieved a significant increase in activity and reached 98.5 % biodiesel yield under optimal conditions, which was 1.3 and 1.6 times higher than that of single immobilized AOL and RML, respectively. Notably, owing to the beneficial synergistic impact of methanol-tolerable AOL and thermal-stable RML, co-im Tween 80-AOL@RML displayed superior activity over single lipase counterparts under excess methanol and variable temperatures. The co-im Tween 80-AOL@RML could maintained 96 % activity after 3 cycles of biodiesel production; however, showed an obvious inactivation after continued reuse. Moreover, methanol-induced denaturation of lipases and glycerol-caused agglomeration of the magnetic nanoparticles during continued transesterification were ascertained by fourier transform infrared analysis and scanning electron microscopy. This study provides new pathways for constructing multi-lipase co-immobilzation as well as an economical and effective biocatalyst for biodiesel production from WCO.
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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2024
·
IF 7.7
Jinhong Gao,Lingli Zhang,Dongxin Zhao,Xin Lu,Qiang Sun,Heng Du,Hongyan Yang,Kui Lu
Aspergillus oryzae β-D-galactosidase (β-Gal) efficiently hydrolyzes sesaminol triglucoside into sesaminol, which has higher biological activity . However, β-Gal is difficult to be separate from the reaction mixture and limited by stability. To resolve these problems, β-Gal was immobilized on amino-functionalized magnetic nanoparticles mesoporous silica pre-activated with glutaraldehyde (Fe 3 O 4 @mSiO 2 -β-Gal), which was used for the first time to prepare sesaminol. Under the optimal conditions, the immobilization yield and recovered activity of β-Gal were 57.9 ± 0.3 % and 46.5 ± 0.9 %, and the enzymatic loading was 843 ± 21 U enzyme /g support . The construction of Fe 3 O 4 @mSiO 2 -β-Gal was confirmed by various characterization methods, and the results indicated it was suitable for heterogeneous enzyme-catalyzed reactions. Fe 3 O 4 @mSiO 2 -β-Gal was readily separable under magnetic action and displayed improved activity in extreme pH and temperature conditions. After 45 days of storage at 4 °C, the activity of Fe 3 O 4 @mSiO 2 -β-Gal remained at 92.3 ± 2.8 %, which was 1.29 times than that of free enzyme, and its activity remained above 85 % after 10 cycles. Fe 3 O 4 @mSiO 2 -β-Gal displayed higher affinity and catalytic efficiency. The half-life was 1.41 longer than free enzymes at 55.0 °C. Fe 3 O 4 @mSiO 2 -β-Gal was employed as a catalyst to prepare sesaminol, achieving a 96.7 % conversion yield of sesaminol. The excellent stability and catalytic efficiency provide broad benefits and potential for biocatalytic industry applications.
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Food Chemistry-X
·
2026
·
IF 9.2
Chunlei Tan,Lei Peng,Xiaolin Huang,Mingming Wang,Hongyu Mu,Feng Zhang,Jun Sheng,Yang Tian,Cunchao Zhao
Co-inoculation with Aspergillus oryzae , Lactobacillus plantarum , and Saccharomyces rouxii significantly improved walnut soy sauce (WSS) quality. 72 volatile compounds (VOCs) and 1972 non-VOCs were identified by headspace-gas chromatography-ion mobility spectrometry (HS-GC-IMS) and liquid chromatography–mass spectrometry (LC-MS), respectively. Compared to single A. oryzae fermentation, S. rouxii co-inoculation increased amino acid nitrogen by 36.1% to 1.13 g/100 mL ( p < 0.05), while L. plantarum elevated total acids by 33% and ketones to 54.7% relative content. Triple co-inoculation fermentation achieved the highest umami (7.8 point) and soy sauce-like flavor (8.2 point) with minimal bitterness. Metabolic pathway analysis revealed that key flavor compounds were associated with glycolysis, organic acid, and amino acid metabolism. These findings provide new insights into optimizing the flavor and quality of WSS through mixed-culture fermentation.
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PREPARATIVE BIOCHEMISTRY & BIOTECHNOLOGY
·
2025
·
IF 1.9
Shuang Jin,Yubin Ren,Hongyao Cai,Biqiong Chen,Yupeng Cheng,Weili Liu,Cailiang Peng,Yujie Fu,Chen Lv,Huiling Li
This study introduces a green, sustainable, and efficient approach for biotransforming sophoricoside into genistein from Fructus Sophorae using Aspergillus oryzae by removal of one molecule of glucose by β-glucosidase, an edible microorganism immobilized on magnetic cellulose and treated with deep eutectic solvents (DES). The goal was to enhance the biotransformation ratio by optimizing reaction conditions and selecting the most suitable DES. Various DESs, including natural deep eutectic solvents (NADES), were assessed for their ability to improve catalytic performance. Among them, the NADES system comprising choline chloride (CHCL) and glycerol (G) exhibited the highest catalytic efficiency (32.19 mg/g) under optimal conditions: temperature 33 °C, time 65 hours, pH 5.5, and a liquid-to-solid ratio of 45:1 (mL/g). This yield was 10.60 times greater than the genistein yield from untreated F. Sophorae. This combination notably increased cell membrane permeability, aiding the bioconversion process. The cellulose immobilization technique provided a stable and reusable microreactor and maintained microbial activity (80.37%) over 10 cycles. These findings validate the bioconversion method as a promising and sustainable strategy for genistein production from plant-derived sophoricoside, with potential applications in pharmaceutical and nutraceutical industries.
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