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学者姓名：洪晶
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Abstract ：
为提高铁观音杀青物的香气物质得率，采用单因素和正交试验对铁观音杀青物的复合酶酶解工艺进行优化，采用顶空固相微萃取结合气相色谱仪-质谱联用对香气成分进行检测。最佳的复合酶增香工艺为：料液比1∶20 g/mL，酸解后加入0.1%的复合酶，调节pH至4.5,60℃酶解3 h。酶解最佳增香样品的香气物质总量达到3926.52μg/L，比空白增长12.63倍。不同酶解工艺条件下香气物质的种类和含量有一定的差异，增香后的香气物质具有突出的铁观音香气特征，整体香味和谐。研究结果可对茶叶香气提取工艺的研究、茶叶深加工、茶叶香精的调配和食品调香及相关茶产业的发展等提供理论指导。
Keyword ：
气相色谱-质谱联用 气相色谱-质谱联用 酶解 酶解 铁观音杀青物 铁观音杀青物 香气 香气
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| GB/T 7714 | 操晓亮 , 薛婉茹 , 庄志雄 et al. 外源酶提高铁观音杀青物香气的工艺优化及其成分分析 [J]. | 中国食品添加剂 , 2024 , (03) : 88-95 . |
| MLA | 操晓亮 et al. "外源酶提高铁观音杀青物香气的工艺优化及其成分分析" . | 中国食品添加剂 03 (2024) : 88-95 . |
| APA | 操晓亮 , 薛婉茹 , 庄志雄 , 谢李玲 , 周培琛 , 伊勇涛 et al. 外源酶提高铁观音杀青物香气的工艺优化及其成分分析 . | 中国食品添加剂 , 2024 , (03) , 88-95 . |
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为研究外源酶对陈年武夷岩茶挥发性成分的影响,运用气相色谱-质谱联用技术(gas chromatography-mass spectrometry,GC-MS)、感官评价和香气活性值(odor activity value,OAV)方法对酶处理后的武夷岩茶进行分析.GC-MS分析结果表明,纤维素酶、果胶酶、漆酶和β-葡萄糖苷酶质量比为2:1:2:3时有利于香气物质的释放,尤其对醇类、酯类及酮类香气物质释放贡献较大.感官评价和OAV值的结果表明,酶的添加能明显提高武夷岩茶的花香、甜香和木香,复合酶的处理效果最佳,其次是β-葡萄糖苷酶.经复合酶处理后己醛、2-己烯醛和(E,E)-2,4-己二烯醛等物质含量降低,OAV减小.上述研究表明,纤维素酶、果胶酶、漆酶、β-葡萄糖苷酶及其复合酶的添加均可明显改善陈年武夷岩茶香气品质.
Keyword ：
β-葡萄糖苷酶 β-葡萄糖苷酶 果胶酶 果胶酶 武夷岩茶 武夷岩茶 气相色谱-质谱法 气相色谱-质谱法 漆酶 漆酶 纤维素酶 纤维素酶 香气活性值 香气活性值
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| GB/T 7714 | 谢李玲 , 薛婉茹 , 李丹阳 et al. 外源酶对陈年武夷岩茶香气品质的改善作用 [J]. | 食品研究与开发 , 2023 , 44 (5) : 155-164 . |
| MLA | 谢李玲 et al. "外源酶对陈年武夷岩茶香气品质的改善作用" . | 食品研究与开发 44 . 5 (2023) : 155-164 . |
| APA | 谢李玲 , 薛婉茹 , 李丹阳 , 周惠媛 , 孟春 , 洪晶 . 外源酶对陈年武夷岩茶香气品质的改善作用 . | 食品研究与开发 , 2023 , 44 (5) , 155-164 . |
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为提高铁观音茶精油的稳定性,利用喷雾干燥法制备稳定的铁观音茶精油微胶囊.通过单因素和正交试验探究壁材的种类和浓度、芯壁比、包埋温度对微胶囊包埋效果的影响,研究微胶囊的分子结构、微观状态和稳定性等.以明胶、阿拉伯树胶和麦芽糊精为壁材(浓度比为1∶1∶1),在壁材浓度1％(w/v),芯壁比为1∶2(w/w),均质温度为50℃条件下,制得精油微胶囊包埋率为97.12％,产率为62.44％.红外光谱分析结果证实铁观音茶精油被成功包埋;扫描电镜分析结果显示微胶囊囊壁结构相对完整,表面光滑;微胶囊的释放动力研究结果表明微胶囊在4,25℃时达到精油缓慢释放的效果.研究为铁观音茶精油的拓展应用提供理论参考和数据支撑.
Keyword ：
壁材 壁材 微胶囊 微胶囊 稳定性 稳定性 结构表征 结构表征 铁观音茶精油 铁观音茶精油
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| GB/T 7714 | 操晓亮 , 薛婉茹 , 庄志雄 et al. 铁观音茶精油微胶囊化制备及结构表征 [J]. | 包装与食品机械 , 2023 , 41 (6) : 40-45,52 . |
| MLA | 操晓亮 et al. "铁观音茶精油微胶囊化制备及结构表征" . | 包装与食品机械 41 . 6 (2023) : 40-45,52 . |
| APA | 操晓亮 , 薛婉茹 , 庄志雄 , 谢李玲 , 叶淑芳 , 孟春 et al. 铁观音茶精油微胶囊化制备及结构表征 . | 包装与食品机械 , 2023 , 41 (6) , 40-45,52 . |
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Abstract ：
为了提高铁观音杀青叶烟用香料中香气物质的得率,采用生物酶对原料进行酶解增香后再提取。采用顶空固相微萃取(HS-SPME)结合气相色谱-质谱联用(GC-MS)技术分析挥发性香气成分含量并进行感官评定。结果表明,先加入柠檬酸酸解再加入复合酶(纤维素酶0.03%、果胶酶0.03%和β-葡萄糖苷酶0.03%)酶解后,芳樟醇、香叶醇、苯乙醇、二氢芳樟醇、α-松油醇和水杨酸甲酯等挥发性香气成分含量显著增加,香气成分的总量也增加,感官品质显著提升。
Keyword ：
增香 增香 外源酶 外源酶 杀青叶 杀青叶 气质联用仪 气质联用仪 茶叶 茶叶 铁观音 铁观音 顶空固相微萃取 顶空固相微萃取 香气成分 香气成分
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| GB/T 7714 | 张峰 , 薛婉茹 , 陈小明 et al. 外源酶提高铁观音杀青叶香气的工艺研究 [J]. | 茶叶通讯 , 2022 , 49 (01) : 80-87 . |
| MLA | 张峰 et al. "外源酶提高铁观音杀青叶香气的工艺研究" . | 茶叶通讯 49 . 01 (2022) : 80-87 . |
| APA | 张峰 , 薛婉茹 , 陈小明 , 谢李玲 , 李斌 , 孟春 et al. 外源酶提高铁观音杀青叶香气的工艺研究 . | 茶叶通讯 , 2022 , 49 (01) , 80-87 . |
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In this study, we attempted to prepare novel angiotensin I-converting enzyme inhibitory (ACEI) peptides from Tie Guanyin tea residue protein (TTRP). Different proteases were used to hydrolyze TTRP to prepare ACEI peptides, neutral protease and alkaline protease hydrolysates exhibited higher ACEI activity and was chosen in further hydrolysis treatment. Response surface methodology (RSM) was used to optimize the enzymatic condition, and the results indicated that the optimal conditions of enzymatic hydrolysis were: 4% (w/v) of TTRP in water was hydrolyzed with 3500 U/g neutral protease at 50 degrees C and pH 6.5 for 2.5 h in the first step and then with 5000 U/g alkaline protease at 50 degrees C and pH 10.0 for 3 h in the second step. Under the optimum condition, the ACE inhibitory rate of the final products was 88.45% +/- 0.45% at the concentration of 1.0 mg/mL. Moreover, ACEI peptides derived from TTRP showed good stability under different temperatures, pHs, metal ions and gastrointestinal digestion. These results indicated that the TTRP has potential to be used for preparing ACEI peptides.
Keyword ：
ACEI peptides ACEI peptides response surface methodology (RSM) response surface methodology (RSM) stability stability Tie Guanyin tea residue protein Tie Guanyin tea residue protein two-step enzymatic hydrolysis two-step enzymatic hydrolysis
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| GB/T 7714 | Ye, Shufang , Luo, Jinyan , Lin, Jiarong et al. Preparation of angiotensin I-converting enzyme (ACE) inhibitory peptides from Tie Guanyin tea residue protein using two-step enzymatic hydrolysis [J]. | FOOD SCIENCE AND TECHNOLOGY , 2022 , 42 . |
| MLA | Ye, Shufang et al. "Preparation of angiotensin I-converting enzyme (ACE) inhibitory peptides from Tie Guanyin tea residue protein using two-step enzymatic hydrolysis" . | FOOD SCIENCE AND TECHNOLOGY 42 (2022) . |
| APA | Ye, Shufang , Luo, Jinyan , Lin, Jiarong , Meng, Chun , Hong, Jing . Preparation of angiotensin I-converting enzyme (ACE) inhibitory peptides from Tie Guanyin tea residue protein using two-step enzymatic hydrolysis . | FOOD SCIENCE AND TECHNOLOGY , 2022 , 42 . |
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In this work, four novel angiotensin I-converting enzyme inhibitory (ACEI) peptides were isolated and identified from peony (Paeonia suffruticosa Andr.) seed hydrolysate (PSH) by consecutive chromatography and UPLC-ESIQTOF-MS/MS. The IC50 values of HWS (0.640 +/- 0.016 mg/mL) and VLSGF (0.328 +/- 0.040 mg/mL) were significantly (p < 0.05) lower than those of the other two peptides. The Lineweaver-Burk plots showed that VLSGF is competitive inhibition against ACE and HWS acted as a mixed-type inhibitor. Meanwhile, the results of molecular docking showed hydrogen interactions between VLSGF/HWS and ACE. In human endothelial cells, the pretreatments of VLSGF and HWS could increase the production of nitric oxide (NO) and the expression of endothelial nitric oxide synthase (eNOS). In addition, they also decreased the reactive oxygen species (ROS) production. These results indicated that it may be possible to use peony seed protein hydrolysate to create ingredients for functional foods.
Keyword ：
ACEI peptides ACEI peptides Human umbilical vein endothelial cells Human umbilical vein endothelial cells inhibitory mechanism inhibitory mechanism molecular docking molecular docking purification purification
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| GB/T 7714 | Ye, Shufang , Chen, Qiuluan , Li, Danyang et al. Isolation and identification of novel angiotensin I-converting enzyme (ACE) inhibitory peptides from Pony Seed and evaluation of the inhibitory mechanisms [J]. | JOURNAL OF FUNCTIONAL FOODS , 2022 , 95 . |
| MLA | Ye, Shufang et al. "Isolation and identification of novel angiotensin I-converting enzyme (ACE) inhibitory peptides from Pony Seed and evaluation of the inhibitory mechanisms" . | JOURNAL OF FUNCTIONAL FOODS 95 (2022) . |
| APA | Ye, Shufang , Chen, Qiuluan , Li, Danyang , Zhou, Huiyuan , Chen, Yanbin , Meng, Chun et al. Isolation and identification of novel angiotensin I-converting enzyme (ACE) inhibitory peptides from Pony Seed and evaluation of the inhibitory mechanisms . | JOURNAL OF FUNCTIONAL FOODS , 2022 , 95 . |
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以奇亚籽粗蛋白为原料,酶解法制备抗氧化肽并通过响应面法优化工艺。同时以1,1-二苯基-2-三硝基苯肼(1,1-diphenyl-2-picrylhydrazyl,DPPH)自由基和羟基自由基清除率为指标,通过单因素试验,筛选最佳酶并考察加酶量、pH值、时间、温度等对产物抗氧化能力的影响。在单因素试验基础上,通过响应面分析法对酶解工艺进一步优化,同时建立酶解工艺的二次项数学模型并验证其可靠性。结果表明:中性蛋白酶为最适酶,酶解最佳工艺为:加酶量3 170 U/g,pH 6.9,酶解时间4.9 h,酶解温度50℃,此时DPPH自由基和羟基自由基清除率分别为54.90%、41.03%,与理论值无显著...
Keyword ：
响应面法 响应面法 奇亚籽 奇亚籽 工艺优化 工艺优化 抗氧化肽 抗氧化肽 酶解 酶解
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| GB/T 7714 | 马倩 , 潘梦莹 , 陈秋銮 et al. 奇亚籽蛋白酶解制备抗氧化肽的工艺优化 [J]. | 食品研究与开发 , 2021 , 42 (03) : 122-129,224 . |
| MLA | 马倩 et al. "奇亚籽蛋白酶解制备抗氧化肽的工艺优化" . | 食品研究与开发 42 . 03 (2021) : 122-129,224 . |
| APA | 马倩 , 潘梦莹 , 陈秋銮 , 陈雪芹 , 孟春 , 洪晶 . 奇亚籽蛋白酶解制备抗氧化肽的工艺优化 . | 食品研究与开发 , 2021 , 42 (03) , 122-129,224 . |
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本发明公开了一种来源于紫苏籽粕的ACE抑制肽及其制备方法与应用。所述ACE抑制肽的氨基酸序列为Val‑Gly‑Ala‑Tyr。通过体外ACE抑制活性测定发现，该紫苏籽粕ACE抑制肽的IC50为0.861 mg/mL，其浓度为0.05 mg/mL时，能有效提高人脐静脉内皮细胞NO的释放量，并且对人脐静脉内皮细胞无毒副作用。本发明提供的紫苏籽粕ACE抑制肽具有结构简单、安全、活性强的特点，且易于进行生产，有望为制备高血压预防药物提供有效成分，或作为功能食品添加剂供高血压患者食用。
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| GB/T 7714 | 洪晶 , 陈雪芹 , 叶淑芳 et al. 一种来源于紫苏籽粕的ACE抑制肽及其制备方法与应用 : CN202110862237.0[P]. | 2021-07-29 . |
| MLA | 洪晶 et al. "一种来源于紫苏籽粕的ACE抑制肽及其制备方法与应用" : CN202110862237.0. | 2021-07-29 . |
| APA | 洪晶 , 陈雪芹 , 叶淑芳 , 陈彦彬 . 一种来源于紫苏籽粕的ACE抑制肽及其制备方法与应用 : CN202110862237.0. | 2021-07-29 . |
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以牡丹籽粕为原料,用酶解法制备ACE抑制肽及其稳定性研究.以血管紧张素转化酶(angiotension converting enzyme,ACE)抑制率为指标,从中性蛋白酶、碱性蛋白酶、胃蛋白酶、胰蛋白酶和风味蛋白酶中筛选出最佳ACE抑制肽制备酶为中性蛋白酶.以单因素实验为基础,进行酶解条件的响应面优化,结果显示牡丹籽ACE抑制肽酶法制备的最优条件为:底物浓度2％,pH7.5,加酶量7200 U/g,酶解温度43℃,酶解时间2h,此时酶解液ACE抑制率可达到86.93％±2.38％.此外,稳定性分析显示该ACE抑制肽具有良好的温度和酸碱稳定性,在温度20 ～ 100℃与pH2～10的环境下,ACE抑制活性没有显著变化(P＞0.05),并且经过体外胃肠模拟消化后,ACE抑制活性变化不显著(P＞0.05),仍能保持良好的抑制活性.
Keyword ：
ACE抑制肽 ACE抑制肽 中性蛋白酶 中性蛋白酶 响应面 响应面 牡丹籽粕 牡丹籽粕 稳定性 稳定性
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| GB/T 7714 | 陈秋銮 , 陈雪芹 , 马倩 et al. 酶解法制备牡丹籽ACE抑制肽及其稳定性 [J]. | 食品工业科技 , 2020 , 41 (19) : 149-156 . |
| MLA | 陈秋銮 et al. "酶解法制备牡丹籽ACE抑制肽及其稳定性" . | 食品工业科技 41 . 19 (2020) : 149-156 . |
| APA | 陈秋銮 , 陈雪芹 , 马倩 , 谢李玲 , 薛婉茹 , 孟春 et al. 酶解法制备牡丹籽ACE抑制肽及其稳定性 . | 食品工业科技 , 2020 , 41 (19) , 149-156 . |
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Mycobacterium tuberculosis (Mtb) is the key devastating bacterial pathogen responsible for tuberculosis. Increasing emergence of multi-drug-resistant, extensively drug-resistant, and rifampicin/isoniazid-resistant strains of Mtb makes the discovery of validated drug targets an urgent priority. As a vital translational component of the protein biosynthesis system, elongation factor Tu (EF-Tu) is an important molecular switch responsible for selection and binding of the cognate aminoacyl-tRNA to the acceptor site on the ribosome. In addition, EF-Tu from Mtb (MtbEF-Tu) is involved in the initial step of trans-translation which is an effective system for rescuing the stalled ribosomes from non-stop translation complexes under stress conditions. Given its crucial role in protein biosynthesis, EF-Tu is identified as an excellent molecular target for drug design. Here, we reported the recombinant expression, purification, biophysical characterization, and structural modeling of the MtbEF-Tu protein. Our results demonstrated that prokaryotic expression plasmids of pET28a-MtbEF-Tu could be expressed efficiently in Escherichia coli. We successfully purified the 6x His-tagged proteins with a yield of 16.8 mg from 1 l of Luria Bertani medium. Dynamic light scattering experiments showed that MtbEF-Tu existed in a monomeric form, and circular dichroism experiments indicated that MtbEF-Tu was well structured. Moreover, isothermal titration calorimetry experiments displayed that the purified MtbEF-Tu protein possessed intermediate binding affinities for guanosine-5-triphosphate (GTP) and GDP. The GTP/GDP-binding sites were predicted by flexible molecular docking approach which reveals that GTP/GDP binds to MtbEF-Tu mainly through hydrogen bonds. Our work lays the essential basis for further structural and functional studies of MtbEF-Tu as well as MtbEF-Tu-related novel drug developments.
Keyword ：
MtbEF-Tu MtbEF-Tu protein biosynthesis protein biosynthesis protein expression and purification protein expression and purification protein-guanine nucleotide interaction protein-guanine nucleotide interaction tuberculosis tuberculosis
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| GB/T 7714 | Yang, Juanjuan , Hong, Jing , Luo, Ling et al. Biophysical characterization and ligand-binding properties of the elongation factor Tu from Mycobacterium tuberculosis [J]. | ACTA BIOCHIMICA ET BIOPHYSICA SINICA , 2019 , 51 (2) : 139-149 . |
| MLA | Yang, Juanjuan et al. "Biophysical characterization and ligand-binding properties of the elongation factor Tu from Mycobacterium tuberculosis" . | ACTA BIOCHIMICA ET BIOPHYSICA SINICA 51 . 2 (2019) : 139-149 . |
| APA | Yang, Juanjuan , Hong, Jing , Luo, Ling , Liu, Ke , Meng, Chun , Ji, Zhi-liang et al. Biophysical characterization and ligand-binding properties of the elongation factor Tu from Mycobacterium tuberculosis . | ACTA BIOCHIMICA ET BIOPHYSICA SINICA , 2019 , 51 (2) , 139-149 . |
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