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25513-46-6

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25513-46-6 Usage

Description

Polyglutamic acid (PGA), a poly amino acid produced by Bacillus spp. is a naturally occurring anionic, water-soluble, biodegradable, non-toxic, viscous, edible biopolymer containing D and L-glutamic acid residues with different industrial applications.

Application

Polyglutamic acid is considered a promising bio-based chemical and is already widely used in the food, medical, and wastewater industries due to its biodegradable, non-toxic, and non-immunogenic properties.

Preparation

The Preparation method of Polyglutamic acid is as follows:poplar sawdust was used to produce Polyglutamic acid. Poplar sawdust was treated with acid and then hydrolyzed with cellulose. The enzymatic hydrolysate was used to produce Polyglutamic acid. Through single factor and orthogonal experiments, the optimum enzymatic conditions were determined as follows: solid-liquid ratio 1:5, enzyme amount 22 FPU/g, pH 5.0 and 53 min. Under the enzymatic hydrolysate medium, the Polyglutamic acid yield reached 30.87 ± 0.44 g/L, which was 5.11% higher than that in glucose medium (29.37 ± 0.43 g/L). In addition, the amount of glucose added to the medium was reduced, which realized the comprehensive utilization of various sugars in sawdust enzymatic hydrolysate.

Definition

ChEBI: A macromolecule composed of repeating gamma-linked L-glutamyl units.

Check Digit Verification of cas no

The CAS Registry Mumber 25513-46-6 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 2,5,5,1 and 3 respectively; the second part has 2 digits, 4 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 25513-46:
(7*2)+(6*5)+(5*5)+(4*1)+(3*3)+(2*4)+(1*6)=96
96 % 10 = 6
So 25513-46-6 is a valid CAS Registry Number.

25513-46-6SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 14, 2017

Revision Date: Aug 14, 2017

1.Identification

1.1 GHS Product identifier

Product name γ-poly(L-glutamic acid) macromolecule

1.2 Other means of identification

Product number -
Other names -

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:25513-46-6 SDS

25513-46-6Relevant articles and documents

Structures and antitumor activities of ten new and twenty known surfactins from the deep-sea bacterium Limimaricola sp. SCSIO 53532

Chen, Min,Chen, Rouwen,Ding, Wenping,Li, Yanqun,Tian, Xinpeng,Yin, Hao,Zhang, Si

, (2022/01/11)

Surfactins are natural biosurfactants with myriad potential applications in the areas of healthcare and environment. However, surfactins were almost exclusively produced by the bacterium Bacillus species in previous reported literatures, together with difficulty in isolating pure monomer, which resulted in making extensive effort to remove duplication and little discovery of new surfactins in recent years. In the present study, the result of Molecular Networking indicated that Limimaricola sp. SCSIO 53532 might well be a potential resource for surfacin-like compounds based on OSMAC strategy. To search for new surfactins with significant biological activity, further study was undertaken on the strain. As a result, ten new surfactins (1–10), along with twenty known surfactins (11–30), were isolated from the ethyl acetate extract of SCSIO 53532. Their chemical structures were established by detailed 1D and 2D NMR spectroscopy, HRESIMS data, secondary ion mass spectrometry (MS/MS) analysis, and chemical degradation (Marfey's method) analysis. Cytotoxic activities of twenty-seven compounds against five human tumor cell lines were tested, and five compounds showed significant antitumor activities with IC50 values less than 10 μM. Furtherly, analysis of structure–activity relationships revealed that the branch of side chain, the esterification of Glu or Asp residue, and the amino acid residue of position 7 possessed a great influence on antitumor activity.

Rational engineering ofAcinetobacter tandoiiglutamate dehydrogenase for asymmetric synthesis ofl-homoalanine through biocatalytic cascades

Diao, Shiqing,Jiang, Shuiqin,Liu, Yan,Sun, Yangyang,Wang, Hualei,Wang, Liuzhu,Wei, Dongzhi

, p. 4208 - 4215 (2021/06/30)

l-Homoalanine, a useful building block for the synthesis of several chiral drugs, is generally synthesized through biocascades using natural amino acids as cheap starting reactants. However, the addition of expensive external cofactors and the low efficiency of leucine dehydrogenases towards the intermediate 2-ketobutyric acid are two major challenges in industrial applications. Herein, a dual cofactor-dependent glutamate dehydrogenase fromAcinetobacter tandoii(AtGluDH) was identified to help make full use of the intracellular pool of cofactors when using whole-cell catalysis. Through reconstruction of the hydrophobic network between the enzyme and the terminal methyl group of the substrate 2-ketobutyric acid, the strict substrate specificity ofAtGluDH towards α-ketoglutarate was successfully changed, and the activity obtained by the most effective mutant (K76L/T180C) was 17.2 times higher than that of the wild-type protein. A three-enzyme co-expression system was successfully constructed in order to help release the mass transfer restriction. Using 1 Ml-threonine, which is close to the solubility limit, we obtained a 99.9% yield ofl-homoalanine in only 3.5 h without adding external coenzymes to the cascade, giving 99.9% ee and a 29.2 g L?1h?1space-time yield. Additionally, the activities of the engineeredAtGluDH towards some other hydrophobic amino acids were also improved to 1.1-11.2 fold. Therefore, the engineering design of some dual cofactor-dependent GluDHs could not only eliminate the low catalytic activity of unnatural substrates but also enhance the cofactor utilization efficiency of these enzymes in industrial applications.

Mechanically Strong Heterogeneous Catalysts via Immobilization of Powderous Catalysts to Porous Plastic Tablets

Li, Tingting,Xu, Bo

supporting information, p. 2673 - 2678 (2021/08/03)

Main observation and conclusion: We describe a practical and general protocol for immobilization of heterogeneous catalysts to mechanically robust porous ultra-high molecular weight polyethylene tablets using inter-facial Lifshitz-van der Waals Interactions. Diverse types of powderous catalysts, including Cu, Pd/C, Pd/Al2O3, Pt/C, and Rh/C have been immobilized successfully. The immobilized catalysts are mechanistically robust towards stirring in solutions, and they worked well in diverse synthetic reactions. The immobilized catalyst tablets are easy to handle and reused. Moreover, the metal leaching of immobilized catalysts was reduced significantly.

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