Publications by authors named "Shireen A A Saleh"

Background: The main obstacle facing the utilization of microbial enzymes in industrial applications is the high cost of production substrates. As a result of the mentioned different wastes (coffee powder waste, dates nawah powder, molokhia stems, pea peels, lemon peels, and corn cobs) were investigated as low-cost nutritional substrates for the production of microbial β-galactosidase in this study. The purification of the enzyme and its kinetic and thermodynamics were investigated.

View Article and Find Full Text PDF

β-Mannanase producing fungus was isolated from coffee powder waste and identified as Aspergillus niger MSSFW (Gen Bank accession number OR668928). Dates nawah powder as industrial and agricultural waste was the most inducer of β-mannanase production. The Plackett-Burman and Central Composite designs were used to improve β-mannanase titer.

View Article and Find Full Text PDF

This research represents a novel study to assess how coculture affects levan yield, structure, bioactivities, and molecular weight. Among the 16 honey isolates, four bacterial strains recorded the highest levan yield. The Plackett-Burman design showed that the coculture (M) of isolates G2 and K2 had the maximum levan yield (52 g/L) and the effective factors were sucrose, incubation time, and sugarcane bagasse.

View Article and Find Full Text PDF
Article Synopsis
  • The study explores the production of cellulase using agricultural waste, specifically Molokhia stems, through the fermentation process using Aspergillus awamori MK788209.
  • Statistical optimization techniques, Plackett-Burman and Central Composite Design, significantly improved cellulase yields by 2.51 and 4.86 times, respectively, and increased sugar recovery from pea peels to 338 mg reducing sugar/ml.
  • The produced cellulase demonstrated high effectiveness not only in breaking down agricultural waste but also in improving the properties of cotton fabrics for textile applications.
View Article and Find Full Text PDF

This study aimed to investigate whether the gastroprotective effects of three types of bacterial levans are correlated with their prebiotic-associated anti-inflammatory/antioxidant potentials. Three levans designated as LevAE, LevP, and LevZ were prepared from bacterial honey isolates; purified, and characterized using TLC, NMR, and FTIR. The anti-inflammatory properties of levan preparations were assessed in LPS-stimulated RAW 264.

View Article and Find Full Text PDF

This study investigates the production of the enzyme cocktail by the isolated fungi Aspergillus flavus B2 (GenBank accession number OL655454) using agricultural and industrial (AI) residues as the sole substrate. Of all the AI residues tested, Jew's mallow stalk was the best inducer substrate for enzyme cocktail production without adding any nutrients. Statistical optimization using Response Surface Methodology enhanced the production by 5.

View Article and Find Full Text PDF

Amidated pectin-polyethylene imine-glutaraldehyde (AP-PEI-GA) immobilizer was prepared. The ideal protocol that should be adopted during the immobilizer preparation was investigated via Box-Behnken design (BBD), and it comprised processing the AP beads with 3.4 % (w/w) PEI solution of pH 9.

View Article and Find Full Text PDF

The bacteriocins produced by lactic acid bacteria (LAB) are attracting attention due to their promising applications in food and pharmaceuticals fields. Hence, a LAB strain, GCNRC_GA15, was isolated from Egyptian goat cheese, and molecularly identified as Lactiplantibacillus plantarum. This strain showed a wide antimicrobial spectrum, which was found to be of proteineous nature, suggesting that L.

View Article and Find Full Text PDF

The object of this study was to utilize agro-industrial waste Corchorus olitorius stems (molokhia stems, MS) as substrate, for Aspergillus niger MK981235 xylanase production and as source of biologically active xylooligosaccharides (XOS). This study succeeded in utilization of Aspergillus niger MK981235 xylanase under different saccharification conditions designed by central composite design (CCD) for extraction of 15 biologically active XOS (anti-hepatotoxic, antioxidant, hypocholesterolemic and prebiotic) with different monosaccharides constituents composition and percent. A.

View Article and Find Full Text PDF

Utilization of agricultural wastes as cheap natural resources for production of bioactive products is currently attracting global attention. For this purpose, this study focused on isolation of Aspergillus wewitschiae MN056175 as promising producer of inulinase, then investigating physiochemical, kinetics and thermodynamics of the obtained inulinase, and its ability to extract bioactive fructo-oligosaccharides (FOS) from Cynara scolymus leaves (artichoke leaves, AL). A.

View Article and Find Full Text PDF

Plaque-related diseases are amongst the most common ailments of the oral cavity. Streptococcus mutans is the causal agent of dental caries in animals and humans and is responsible for the formation and accumulation of plaques. This study aimed to identify and evaluate the role of the dental plaque isolates and its surrounding environment in plaque formation or inhibition.

View Article and Find Full Text PDF

314 strain was able to utilize agricultural and industrial wastes for metallo-protease production. Orange peel and wheat bran were found as the most suitable carbon and nitrogen sources, respectively. Optimized production process enhanced the enzyme production by 5.

View Article and Find Full Text PDF

Enzyme cost, stability and its thermodynamic characteristics are the main criteria for industrial use. In this study, Aspergillus awamori amylase was constitutively produced using various agro-industrial wastes. Olive oil cake gave the highest activity (230U/g).

View Article and Find Full Text PDF

Aspergillus niger β-glucosidase was modified by covalent coupling to periodate activated polysaccharides (glycosylation). The conjugated enzyme to activated starch showed the highest specific activity (128.5 U/mg protein).

View Article and Find Full Text PDF