A promising orphan target to treat HD

Ratna, Nikhil

doi:10.1002/mds.27512

Cited by 1 publication

(1 citation statement)

References 4 publications

(4 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The residual activity declined to 46% at 80°C after 1 hour. Researchers like Miyazaki [29], Yan et al [4], Ahmed et al [1], Lee and Lee [5], Ratna et al [30] have reported optimal activity of arabinofuranosidase enzyme ranging from 50-90°C. The source from which the enzyme is produced and characterized from may account for the variation in its optimum temperature be an indication of its activity at different temperature [2].…”

Section: Discussionmentioning

confidence: 99%

A Thermostable and Alkalitolerant Arabinofuranosidase by Streptomyces lividus

Olajide

Adesina

Onilude

2020

BJI

View full text Add to dashboard Cite

Aim: The study aimed at producing and purifying thermostable and alkalitolerant microbial arabinofuranosidase using local Palm Kernel Cake (PKC) as substrate. Study Design: This is an experimental design in which samples were collected thrice and subjected to laboratory analyses from which quantitative data were obtained and analysed. Place and Duration of Study: Ibadan, Nigeria, Five months. Methodology: Bacterial strains were isolated from degrading PKC by serial dilution and pour plate technique on formulated Modified Basal Salt Agar Medium and incubated at 50°C for enzyme activity screening. Plates were afterwards flooded with 1% congo red solution for visualization of hydrolysis zone. Its arabinofuranosidase activity was optimized in solid state fermentation in PKC. Production temperature, pH, moisture content, inoculum size and agitation were studied for optimization test. Optimal production temperature and pH for arabinofuranosidase by isolate was 45°C and pH 9. Produced arabinofuranosidase was purified to apparent homogeneity with ammonium sulphate precipitation, dialysis and column chromatography techniques. Stability of arabinofuranofuranosidase obtained to temperature, pH, substrate concentration and some ions was determined as well as its molecular weight using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Results: Isolate with highest arabinofuranosidase activity was selected and identified as Streptomyces lividus. Purity level attained was 16.36 fold. Enzyme had a specific activity of 25.4 U/mg, and total enzyme activity of 13.2 U. Molecular weight of enzyme appeared as a band of 30 kDa. Purified arabinofuranosidase enzyme revealed optimum temperature and pH as 60oC and 9 respectively. Enzyme was stable over a broad pH range of 3-11, and temperature of 30-80oC. Residual activity after incubating for 1 hour at 70oC was 64%. Enzyme kinetics studies showed Km and Vmax values for P-nitrophenyl arabinofuranoside were 2.3mM and 0.7U/min respectively. Conclusion: Apart from Solid State Fermentation (SSF) of PKC being a potential fermentation technique for production of arabinofuranosidase by Streptomyces lividus, the enzyme was highly stable.

show abstract