RESUMEN
Water-soluble polysaccharides were extracted from potato peel waste (PPW). The structure of the polysaccharides from PPW (PPPW) was examined by means of Fourier transform-infrared spectroscopy (FT-IR) analysis, X-ray diffractometry (XRD) and gas chromatography-mass spectrometry (GC-MS). The results suggest that the extracted polysaccharides form a semi-crystalline polymer constituted essentially of the functional groups CO, CH and OH. Acid hydrolysis of this polymer yielded glucose (76.25%) as the dominant sugar functional properties (water holding capacity: WHC, oil holding capacity: OHC, foaming, and emulsion properties) of this polymer were studied. The PPPW showed interesting water-holding and fat-binding capacities which were 4.097 ± 0.537 g/g and 4.398 ± 0.04 g/g, respectively. In addition, it presented good foaming and emulsion properties. The antioxidant activity of this polymer was also studied and revealed that the polysaccharides showed interesting 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical-scavenging capacity (IC50 PPPW=11.578 mg/mL), reducing power and ß-carotene bleaching inhibition activities, and also a strong ABTS radical scavenging activity (IC50 PPPW=2mg/mL). Overall, the results suggest that the polysaccharide is a promising source of natural antioxidants and can be used as additive in food, pharmaceutical and cosmetic preparations.
Asunto(s)
Antioxidantes/análisis , Raíces de Plantas/química , Polisacáridos/análisis , Solanum tuberosum/química , Agua/química , Antioxidantes/química , Antioxidantes/farmacología , Benzotiazoles/química , Compuestos de Bifenilo/química , Carbohidratos de la Dieta/análisis , Carbohidratos de la Dieta/farmacología , Emulsiones , Cromatografía de Gases y Espectrometría de Masas , Oxidación-Reducción , Picratos/química , Polisacáridos/química , Polisacáridos/farmacología , Espectroscopía Infrarroja por Transformada de Fourier , Ácidos Sulfónicos/química , beta Caroteno/químicaRESUMEN
The highest beta-mannanase activity was produced by Penicillium occitanis Pol6 on flour of carob seed, whereas starch-containing medium gave lower enzymes titles. The low molecular weight enzyme was purified to homogeneity by ammonium sulfate precipitation, gel filtration, and ion-exchange chromatography procedures. The purified beta-mannanase (ManIII) has been identified as a glycoprotein (carbohydrate content 5%) with an apparent molecular mass of 18 kDa. It was active at 40 degrees C and pH 4.0. It was stable for 30 min at 70 degrees C and has a broad pH stability (2.0-12.0). ManIII showed K (m), V (max), and K (cat) values of 17.94 mg/ml, 93.52 U/mg, and 28.13 s(-1) with locust bean gum as substrate, respectively. It was inhibited by mannose with a K (I) of 0.610(-3) mg/ml. ManIII was activated by CuSO4 and CaCl2 (2.5 mM). However, in presence of 2.5 mM Co2+, its activity dropped to 60% of the initial activity. Both N-terminal and internal amino acid sequences of ManIII presented no homology with mannanases of glycosides hydrolases. During incubation with locust bean gum and Ivory nut mannan, the enzyme released mainly mannotetraose, mannotriose, and mannobiose.
Asunto(s)
Manosidasas/aislamiento & purificación , Manosidasas/metabolismo , Penicillium/enzimología , Secuencia de Aminoácidos , Cationes Bivalentes/farmacología , Galactanos/metabolismo , Cinética , Mananos/metabolismo , Peso Molecular , Gomas de Plantas/metabolismoRESUMEN
A new thermophilic bacterial strain identified as Bacillus cohnii US147 was isolated from the southern Tunisian soil. The identification was based on physiological tests and molecular techniques related to the 16S ribosomal ribonucleic acid. The isolated strain produced amylase, which was purified. This amylase had an apparent molecular mass of 30 kDa as estimated by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. Amylase US147 showed K (m) and V (max) values of 0.7 mg/ml and 2.2 U/ml, respectively, with starch as the substrate. The enzyme was active in acid and basic pH and had a maximal activity on starch at pH 9 and 70 degrees C. The enzyme was stable at pH 9 for 72 h and retained half of its activity after incubation at 70 degrees C for 150 min. A partially inhibition (15%, 25%, 23%, 20%, and 22%) was obtained with 1 mM SDS, 1 mM NaBO(3), 1 mM H(2)O(2,) 1 mM Zn(+2), and 5 mM ethylenediamine tetraacetic acid (EDTA), respectively. The amylase recovered its original activity by the addition of 10 mM Ca (2+) to the 5 mM EDTA. These properties indicated a possible use of this amylase in starch saccharification, in detergent, and in other industrial applications.