Naringinase
(Synonyms: 柚苷酶) 目录号 : GC61697
Naringinase是一种水解酶复合物，具有α-L-鼠李糖苷酶和β-D-葡萄糖苷酶的活性。Naringinase在自然界中广泛存在。Naringinase可用于类固醇，抗生素的生物转化，主要用于糖苷的水解。
Cas No.:9068-31-9
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Naringinase, a hydrolytic enzymatic complex, possesses the activity of both α-L-rhamnosidase and β-D-glucosidase. Naringinase has wide occurrence in nature. Naringinase can be used in the biotransformation of steroids, antibiotics, and mainly on glycosides hydrolysis[1][2].
Naringinase is used in orange and grapefruit processing to improve pulp washing, increase the recovery yield of essential oils, and to debitter and clarify the juice[1].Naringinase can be used in the deglycosylation of glycopeptide antibiotics, flavonoids, or glycolipids[2].
[1]. Puri M, et, al. Production, purification, and characterization of the debittering enzyme naringinase. Biotechnol Adv. 2000 May;18(3):207-17. [2]. Ribeiro MH. Naringinases: occurrence, characteristics, and applications. Appl Microbiol Biotechnol. 2011 Jun;90(6):1883-95.
| Cas No. | 9068-31-9 | SDF | |
| 别名 | 柚苷酶 | ||
| Canonical SMILES | [Naringinase] | ||
| 分子式 | 分子量 | ||
| 溶解度 | Water: 120 mg/mL | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Naringinase Biosynthesis by Aspergillus niger on an Optimized Medium Containing Red Grapefruit Albedo
Molecules 2022 Dec 10;27(24):8763.PMID:36557896DOI:10.3390/molecules27248763.
This study aimed to develop a method of Naringinase biosynthesis by Aspergillus niger KMS on an optimized culture medium. The concentration of the six medium components in shake flasks was optimized by the Box and Wilson factor gradient method. Naringinase's substrate, naringin, powdered albedo, flavedo, and red grapefruit segment membranes were used to stimulate Naringinase biosynthesis. Rhamnose was chosen as the carbon source, while the nitrogen source was yeast extract and sodium nitrate. Naringinase biosynthesis was most favorable in the culture medium with the following composition (g 100 mL): 3.332-NaNO3; 3.427-yeast extract; 0.184-KH2PO4; 0.855-red grapefruit albedo; 0.168-naringin; 2.789-rhamnose. The obtained Aspergillus niger KMS culture fluid was concentrated, thereby precipitating the protein. As a result, a Naringinase preparation with high activity, equal to 816 µmol × min-1 × g-1, was obtained.
Immobilization of Naringinase from Aspergillus Niger on a Magnetic Polysaccharide Carrier
Molecules 2020 Jun 12;25(12):2731.PMID:32545562DOI:10.3390/molecules25122731.
Naringinase is an enzymatic complex used in the deglycosylation of compounds with a high application potential in the food and pharmaceutical industries. The aim of the study was to immobilize Naringinase from Aspergillus niger KMS on a magnetic carrier obtained on the basis of carob gum activated by polyethyleneimine. Response surface methodology was used to optimize Naringinase immobilization taking into account the following factors: pH, immobilization time, initial concentration of Naringinase and immobilization temperature. The adsorption of the enzyme on a magnetic carrier was a reversible process. The binding force of Naringinase was increased by crosslinking the enzyme with the carrier using dextran aldehyde. The crosslinked enzyme had better stability in an acidic environment and at a higher temperature compared to the free form. The immobilization and stabilization of Naringinase by dextran aldehyde on the magnetic polysaccharide carrier lowered the activation energy, thus increasing the catalytic capacity of the investigated enzyme and increasing the activation energy of the thermal deactivation process, which confirms higher stability of the immobilized enzyme in comparison with free Naringinase. The preparation of crosslinked Naringinase retained over 80% of its initial activity after 10 runs of naringin hydrolysis from fresh and model grapefruit juice.
A facile preparation of immobilized Naringinase on polyethyleneimine-modified Fe3O4 magnetic nanomaterials with high activity
RSC Adv 2021 Apr 19;11(24):14568-14577.PMID:35424008DOI:10.1039/d1ra01449h.
Polyethyleneimine-modified Fe3O4 nanoparticles (Fe3O4-PEI) were synthesized by the one-step co-precipitation method, and the resulting material was used to immobilize Naringinase from the fermentation broth of Aspergillus niger FFCC uv-11. The immobilized Naringinase activity could reach up to 690.74 U per g-support at the conditions of initial Naringinase activity of 406.25 U mL-1, immobilization time of 4 h, glutaraldehyde concentration of 40% (w/v), immobilization temperature of 35 °C, and pH value of 5.5, with naringinase-carrying rate and Naringinase activity recovery of 92.93% and 20.89%, respectively. In addition, the immobilized Naringinase exhibited good pH and temperature stability in a pH range of 3.5-6.0 and temperature range of 40-70 °C, and the optimal reaction pH and reaction temperature were optimized as 5.5 and 60 °C, respectively. Besides, the immobilized Naringinase could maintain 60.58% of the original activity after 10 reuse cycles, indicating that the immobilized Naringinase had good reusability. Furthermore, the immobilized Naringinase also performed excellent storage stability, 87.52% of enzyme activity still remained as stored at 4 °C for one month. In conclusion, the Fe3O4-PEI could be considered as a promising support for Naringinase immobilization, with the advantages of high enzyme activity loading, good reusability, storage stability and rapid recovery.
Updates on Naringinase: structural and biotechnological aspects
Appl Microbiol Biotechnol 2012 Jan;93(1):49-60.PMID:22080346DOI:10.1007/s00253-011-3679-3.
Naringinases has attracted a great deal of attention in recent years due to its hydrolytic activities which include the production of rhamnose, and prunin and debittering of citrus fruit juices. While this enzyme is widely distributed in fungi, its production from bacterial sources is less commonly known. Fungal Naringinase are very important as they are used industrially in large amounts and have been extensively studied during the past decade. In this article, production of bacterial Naringinase and potential biotechnological applications are discussed. Bacterial rhamnosidases are exotype enzymes that hydrolyse terminal non-reducing α-L-rhamnosyl groups from α-L-rhamnose containing polysaccharides and glycosides. Structurally, they are classified into family 78 of glycoside hydrolases and characterized by the presence of Asp567 and Glu841 in their active site. Optimization of fermentation conditions and enzyme engineering will allow the development of improved rhamnosidases for advancing suggested industrial applications.
Optimization of process parameters for Naringinase production by Aspergillus tubingensis UA13 and pilot scale-up study
Prep Biochem Biotechnol 2022;52(2):226-233.PMID:34033527DOI:10.1080/10826068.2021.1925914.
To improve the Naringinase production of Aspergillus tubingensis UA13, shorten the fermentation period, and verify its industrial application value, Naringinase production conditions were optimized, and 5 L scale-up study in stirred tank bioreactor was carried out. Parameters, including carbon, nitrogen sources and inducer, optimal seed age, inoculum amount, temperature and pH, were adjusted and optimized in shaking flask. Keeping pH at the optimal value 6 in bioreactor, dissolved oxygen was monitored during the fermentation and the optimal stirring rate was investigated. In 5 L scale-up study, the highest Naringinase activity was 72.62 U/mL, which was 1.75 times higher than that (41.52 U/mL) in shaking flask and the fermentation period was shortened by 24 h.