Kondepudi Kanthi Kiran

Bio: Kondepudi Kanthi Kiran is an academic researcher from Indian Institute of Technology Madras. The author has contributed to research in topics: Amylase & Alpha-amylase. The author has an hindex of 1, co-authored 1 publications receiving 110 citations.

Production of surfactant and detergent-stable, halophilic, and alkalitolerant alpha-amylase by a moderately halophilic Bacillus sp. Strain TSCVKK.

Abstract: A moderately halophilic alkalitolerant Bacillus sp. Strain TSCVKK, with an ability to produce extracellular halophilic, alkalitolerant, surfactant, and detergent-stable alpha-amylase was isolated from soil samples obtained from a salt-manufacturing industry in Chennai. The culture conditions for higher amylase production were optimized with respect to NaCl, substrate, pH, and temperature. Maximum amylase production of 592 mU/ml was achieved in the medium at 48 h with 10% NaCl, 1% dextrin, 0.4% yeast extract, 0.2% tryptone, and 0.2% CaCl2 at pH 8.0 at 30 °C. The enzyme activity in the culture supernatant was highest with 10% NaCl at pH 7.5 and 55 °C. The amylase that was partially purified by acetone precipitation was highly stable in various surfactants and detergents. Glucose, maltose, and maltooligosaccharides were the main end products of starch hydrolysis indicating that it is an alpha-amylase.

Isolation and characterization of novel α-amylase from marine Streptomyces sp. D1

Abstract: In this study, we have reported novel α-amylase enzyme from less extensively studied marine Streptomyces sp. D1. Enzyme production was determined by using media containing 2% sucrose, 0.35% peptone and 0.15% of malt extract. Optimum temperature for enzyme production and activity was found to be 45 °C and enzyme retained almost 50% of its activity at 85 °C. Enzyme activity was also retained in presence of commercially available detergent and oxidizing agents. The partially purified enzyme from strain D1 exhibited specific activity of 113.64 U/mg protein that corresponds to 2.8-fold purification. SDS-PAGE and zymogram activity staining showed a single band equal to molecular mass of 66 kDa. The reported enzyme may have wide spread application for detergent and pharmaceutical industry.

Characterization and stability studies on surfactant, detergent and oxidant stable α-amylase from marine haloalkaliphilic Saccharopolyspora sp. A9

Abstract: A halopalkaliphilic marine Saccharopolyspora sp. stain A9 with an ability to produce surfactants, oxidant and detergent stable α-amylase was isolated from marine sediments collected from west coast of India. The α-amylase from strain A9 was purified to homogeneity with the aid of ammonium sulfate precipitation and gel filtration chromatography by using Sephadex G-75, insoluble corn starch and sephacryl S-100 column, with a 39.01-fold increase in specific activity. SDS-PAGE and zymogram activity staining showed a single band equal to molecular mass of 66 kDa. Enzyme was found to be stable in presence of wide range of NaCl concentration with maximum activity found at 11% (w/v) of NaCl. Enzyme showed remarkable stability towards laboratory surfactants, detergents and oxidants. Glucose, maltose and maltotriose were the main end product of starch hydrolysis, indicating it is α-amylase.

Purification and characterization of an organic-solvent-tolerant halophilic α-amylase from the moderately halophilic Nesterenkonia sp. strain F.

Abstract: A halophilic α-amylase produced by Nesterenkonia sp. strain F was purified to homogeneity by 80% ethanol precipitation, Q-Sepharose anion exchange, and Sephacryl S-200 gel filtration chromatography. The purified amylase exhibited specific activity of 357 unit/mg protein that corresponds to twofold purification. The molecular mass of the amylase was determined to be 57 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and gel filtration chromatography. The optimal pH and temperature for enzyme activity were 6.5 and 45°C, respectively. The amylase was active over a wide range of salt concentrations (0–4 M) with maximum activity at 0.75–1 M NaCl. The α-amylase activity was stimulated by Ca2+ and inhibited by ethylenediamine tetraacetic acid (EDTA), suggesting that this enzyme is a metalloenzyme. The purified enzyme showed remarkable stability towards surfactants (Tween 20, Tween 80, and Triton X-100), and its activity was increased by β-mercaptoethanol. The halophilic α-amylase was stable in the presence of various organic solvents such as benzene, chloroform, toluene, and cyclohexane. These properties indicate wide potential applications of this α-amylase in starch-processing industries.