Purification and characterization of the indicator calmagite

A scheme for the purification of the azo dye calmagite is described which involves solvent extraction, column partition chromatography, and adsorption chromatography on a nonpolar adsorbent. The final product, analyzed by thin-layer chromatography and by acid–base and ion-pair titrations, is of >99% purity. Molar absorptivities and acid ionization constants are reported for the conjugate species.

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Optimization, purification and characterization of α-glucosidase inhibitors from Streptomyces costaricanus EBL.HB6 isolated in Vietnam

10.21203/rs.3.rs-931347/v1 ◽

2021 ◽

Author(s):

Thi Trung Nguyen ◽

Thi Hong Thao Phan ◽

Phuong Dai Nguyen Nguyen ◽

Thi Mai Anh Dao ◽

Van Hien Mai ◽

...

Keyword(s):

Inhibitory Activity ◽

Retention Factor ◽

Cultivation Conditions ◽

Purification And Characterization ◽

Glucosidase Inhibitors ◽

Rrna Sequencing ◽

Initial Ph ◽

Layer Chromatography ◽

Great Burden

Abstract BackgroundDiabetes, a disease that has been a great burden of the treatment cost for patients and society. There are many drugs have been used to cure this disease available on the pharmaceutical market. One of the most prevalent source to produce these compounds are microorganism. Among them, Streptomyces sp. are popular microorganisms used for the production of α-glucosidase inhibitors (AGIs). Methods and ResultsIn this study, different cultivation conditions were optimized to enhance the production of AGIs. Purification and evaluation of AGIs from S. costaricanus EBL.HB6 were also performed. Our results demonstrated that Streptomyces costaricanus EBL.HB6 had the highest α-glucosidase inhibitory activity among 6 Streptomyces sp. strains were isolated in Vietnam. The 16S rRNA sequencing of isolating HBC6-2 indicated 99% identity to the corresponding sequence of Streptomyces costaricanus, and was registered on GenBank with the code MT 453944.1. Streptomyces costaricanus EBL.HB6 was able to produce melanin yellow pigment, and its aerial and substrate mycelia have brown and yellow-grey pigment on ISP2 cultivating medium, respectively. The α-glucosidase inhibitory activity of the supernatant was increased by a factor of 1.2 under optimal conditions (media containing 1.5% glucose, 1.2% yeast extract at 28°C, initial pH of 6.5, and culture time for 120 h) in comparison with the initial media and condition. The purified efficacy of a-glucosidase inhibitors was 5% with a retention factor of 0.71 on thin-layer chromatography and IC50 value of 9.59 mg/mL.ConclusionsStreptomyces costaricanus EBL.HB6 strain was selected, purified and evaluated for its highly producible of α-glucosidase inhibitors.

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Purification and characterization of a novel abundant protein in rat bile that binds azo dye metabolites and copper

Biochimica et Biophysica Acta (BBA) - General Subjects ◽

10.1016/0304-4165(83)90184-8 ◽

1983 ◽

Vol 759 (1-2) ◽

pp. 23-31 ◽

Cited By ~ 15

Author(s):

Audrey R. Samuels ◽

Jonathan H. Freedman ◽

Madhu M. Bhargava

Keyword(s):

Azo Dye ◽

Purification And Characterization ◽

Abundant Protein ◽

Rat Bile

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Puriﬁcation and Characterization of a Yam Glycoprotein Isolated by Alkaline Extraction from Yam Tuber

Advanced Materials Research ◽

10.4028/www.scientific.net/amr.560-561.368 ◽

2012 ◽

Vol 560-561 ◽

pp. 368-373

Author(s):

Li Ming Zhang ◽

Yan Qiao Wang ◽

Li Chao Zhang ◽

Shu Li Man ◽

Bei Mei Zuo

Keyword(s):

Functional Foods ◽

Gel Filtration ◽

Processing Method ◽

Purification And Characterization ◽

Automatic Amino Acid Analyzer ◽

Sds Page ◽

Amino Acid Analyzer ◽

Layer Chromatography ◽

Protein Moiety

Yam glycoprotein (YGP) is an important source of bioactives for functional foods. To investigate the effects of alkaline extracting method on the features of YGP, A glycoprotein was isolated from yam tubers by using alkaline processing method, and purified by ion-exchange and gel filtration column chromatography. During the SDS-PAGE eletrophoresis, the result shows a band with approximately 30 kDa molecular weight. The YGP consists of protein moiety (62.34%) and carbohydrate moiety (37.51%), respectively. By the automatic amino acid analyzer detecting, it indicated that the YGP consists of 17 kinds of amino acids and contains a high percentage of glutamic acid and aspartic acid. The results of thin-layer chromatography show that oligosaccharides of the YGP contain D-glucose, D-galactose and mannose.

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Application of thin-layer chromatography to the purification and characterization of some methyl glucosides

Journal of Chromatography A ◽

10.1016/s0021-9673(01)80036-4 ◽

1971 ◽

Vol 59 (1) ◽

pp. 231-233 ◽

Cited By ~ 3

Author(s):

Patrich J. Brennan

Keyword(s):

Thin Layer ◽

Thin Layer Chromatography ◽

Purification And Characterization ◽

Layer Chromatography

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Partial Purification and Characterization of Endoxylanase from a fungus, Leohumicola incrustata

Bio-Research ◽

10.4314/br.v19i1.2 ◽

2021 ◽

Vol 19 (1) ◽

pp. 1192-1201

Author(s):

Olusegun Richard Adeoyo ◽

Brett Ivan Pletschke ◽

Joanna Felicity Dames

Keyword(s):

Industrial Applications ◽

Glycoside Hydrolases ◽

Precipitation Method ◽

Partial Purification ◽

Purification And Characterization ◽

Ammonium Sulphate Precipitation ◽

Incubation Periods ◽

Rf Values ◽

Layer Chromatography

Xylanases are glycoside hydrolases (GH) that degrade β-1,4-xylan, a linear polysaccharide found as hemicellulose in cell wall of plants. Endoxylanase (Endo-1,4-β-xylanase, EC 3.2.1.8) randomly catalyses xylan to produce varying short xylooligosaccharides (XOS). This study aimed to determine the characteristics of a partially purified endoxylanase from Leohumicola incrustata. Enzyme production was carried out using beechwood (BW) xylan, after which the cell-free crude filtrate was concentrated using the ammonium sulphate precipitation method. The hydrolysed products were analysed by thin-layer chromatography (TLC) and zymography. The result showed that the enzyme produced varying smaller-sized linear xylooligosaccharides with Rf values corresponding to those of xylobiose, xylotriose, xylotetraose, xylopentaose, xylohexaose and other higher oligomers. The endoxylanase had a molecular mass of 72 kDa. The enzyme is stable in the presence of K+, Na+, Ca2+, Fe2+, Mg2+, Zn2+, Co2+, pH of 5.0 and temperature of 37oC. However, the activity gradually decreased after 60 min at 50oC and retained over 69% activity after 120 min, while at 60 and 70oC, the enzyme activity sharply decreased (pre-incubation periods). Endoxylanase from L. incrustata is comparable to those of other microorganisms and should be considered an attractive candidate for future industrial applications.

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