Amalendu Sinhababu

Extraction and chemical investigation of Kulthi (Macrotylona uniflorus, Lam.) seed protein

Studies have been carried out on the protein solubility profile of Kulthi (Macrotylona uniflorus, Lam.) seed in aqueous solution over various pHs and at different concentrations of NaCl, Na2SO3, CaCl2, and MgCl2 at pH 8.0. Amino acid analysis of isolated protein identified 17 amino acids, 9 of which are essential. Gel-permeation chromatography on Sephadex G-200 revealed the presence of seven components in the protein fraction. Their molecular weights were determined by two comparable standard methods. Extractable Kulthi seed proteins in salt solutions were separated electrophoretically into eight fractions whose molecular weights were found to be 186,200, 131,800, 108,400, 91,200, 53,700, 44,700, 38,000, and 27,500.

Novel spray reagent for the identification of amino acids on thin-layer chromatography plates

The detection or identification of amino acids is extremely important for the evaluation of protein structure and also because of their presence in numerous natural products. A new spray reagent, dichlorodicyanobenzoquinone, can produce various distinguishable colours with amino acids. The detection limits for amino acids with this spray reagent ranges between 0.1 and 1.0 µg under cold conditions and also after heating.

Identification of amino acids with modified ninhydrin reagents on thin-layer chromatography plates

The four new spray reagents (Benzoic acid and some of its parahaloderivatives) have been introduced. These reagents enable convenient and easy detection of amino acids on thin-layer chromatography plates by developing distinguishable colors with very high sensitivity.

Modified ninhydrin reagents to detect colors of amino acid zones on thin-layer chromatographic plates

Amino acids are the building units of proteins. Identification of amino acids is extremely important for the evaluation of protein structure and also for the determination of the presence of amino acids in various natural products. Several methods to determine amino acids in biological and pharmaceutical samples have been reported. Thin-layer chromatography (TLC) is one of the most widespread analytical techniques used in the separation and identification of amino acids because it is an inexpensive method and consume only small amounts of samples and solvents. Various stationary phases are available, although silica gel is used by far the most widely. There are also different mobile phases for chromatogram development. Thin-layer chromatography is widely used for the identification of amino acids by various spray reagents [1–22]. Among these, ninhydrin is the most popular because of its high sensitivity [23]. However, ninhydrin produces the same purple/violet color with most amino acids (only proline and hydroxyproline produce yellow color).

Isolation, fractionation, and some chemical studies on Kleinhovia hospita Linn. seed protein

ABSTRACT Protein was extracted from the seeds of Kleinhovia hospita Linn., which is being a nonconventional source. Extraction of K. hospita seed protein at various pH values in aqueous solution and at pH 7, different salt concentrations were done. Fractionation of protein from seeds was performed to separate albumin, globulin, prolamin, and glutelin. The amino acid compositions of total protein isolate (TPI) and the fractions were determined. A total of 15 amino acids were identified including 9 essential amino acids. Gel filtration by Sephadex G-100 revealed the presence of three components in the TPI. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis analysis of TPI and fractions showed different polypeptide bands having molecular weights ranging from 12 to 42 kDa approximately. Scanning electron microscopic study of TPI and fractions revealed the surface topology of the protein.

Identification of Amino Acids on TLC Plates by a Novel Spray Reagent

Abstract Spray reagents are very useful for detecting amino acids on thin layer chromatoplates. Although ninhydrin is most widely used as a spray reagent for identification of amino acids due to its high sensitivity but it produces same purple/violet color with all amino acids, except proline and hydroxyproline. To solve this color problem a new spray reagent, pyrrole-2-carbaldehyde has been introduced, which is capable of producing various distinguishable colors with moderately high sensitivity (0.20-5.0 µg). The reagent in combination with ninhydrin is also capable of developing several distinguishable colors with very high sensitivity (0.06-0.60 µg).

Study of genotypic variation of cultivars of winged bean [Psophocarpus tetragonolobus (Stickm.) DC.] with the help of n-alkane profile

The leaf cuticle is covered by epicuticular wax consisting mainly of straight-chain aliphatic hydrocarbons with a variety of substituted groups. Studies have been concentrated on n-alkanes in epicuticular wax of Winged bean [Psophocarpus tetragonolobus (Stickm.) DC.]. Hydrocarbon constituents especially n-alkane analyses of seven cultivars of Winged bean [Psophocarpustetragonolobus (Stickm.) DC.] have been undertaken. All the n-alkanes in between C14–C18 and C20–C38 are present in each of the species. Among the species, amount of n-alkanes is maximum in IC112417 and relatively low in EC38825. Scanning electron microscopic views were also taken for epicuticular layers and their hydrocarbons of the leaves of all the genotype species of the plant. Qualitative and quantitative characterization of n-alkanes present in the epicuticular wax extracted from the mature leaves can be used as an effective tool in chemo taxonomical work and also for the study of genotypic variation of the different cultivars.

Solubility and Functional Properties of Kleinhovia hospita Linn. Seed Protein Isolate

Abstract Nitrogen solubility, protein content and functional properties of Kleinhovia hospita Linn. seed protein isolate were investigated. Maximum solubility of total protein isolate (TPI) was 94.11 % (± 0.37) at pH 12 where as minimum solubility was 55.15 % (± 0.08) at pH 4. Physico-chemical properties of seed protein isolate were also investigated. The emulsifying capacity, emulsion stability, foaming capacity and foaming stability were greatly affected by pH levels. The protein isolate was highly viscous at different concentrations (pH 7) and at a particular concentration (1.5 %) of different pHs. The water and oil holding capacities were measured as 3.82 g/g (± 0.14) and 2.25 g/g (± 0.11) respectively at a fixed pH 7. The least gelation capacities were 12 % (w/v) in distilled water and 10 % (w/v) in 0.5 M NaCl at pH 7.