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( Adriana M. Rangel-rodriguez ),( J. Adriana Sañudo-barajas ),( Nagamani Balagurusamy ),( Louise Wicker ),( Rosabel Velez-de-la-rocha ),( Juan Carlos Contreras-esquivel ) 한국키틴키토산학회 2018 한국키틴키토산학회지 Vol.23 No.2
In this work, the preparation and characterization of water-soluble polysaccharides from chitosan and Aloe vera was studied. The water-soluble polysaccharides were used to study polyelectrolyte complexes. The reaction time effect for chitosan hydrolysis by endo-chitosanase was studied at 40ºC and pH 5.00 to produce water soluble chitosan (WSCh). The physico-chemical characteristics of chitosan hydrolysates, water-soluble A. vera polysaccharides and polyelectrolyte complexes were determined. After 3 h of chitosan processing, a viscosity reduction of 90%, while only 2.3% of reducing sugars were released. A WSCh was recover by ultrafiltration (1 kDa) from chitosan hydrolysate after 12 h and was spray-dried with a yield of 9.7%. Cold-water extraction of A. vera mucilage from pulp gives a crude polysaccharide yield of 0.81 g/kg (wet basis) based on whole leaf weight. The water isolated mucilage is composed of a mixture of protein and mannan rich-polysaccharide. The results show WSCh’s association capacity with A. vera mucilage by electrostatic interaction.
( Cecilia Perez-cruz ),( Carlos N. Cano-gonzalez ),( Jose Fuentes ),( Nagamani Balagurusamy ),( Carolina E. Vita ),( Roque A. Hours ),( Cristobal N. Aguilar ),( Sebastian F. Cavalitto ),( Juan C. Cont 한국키틴키토산학회 2018 한국키틴키토산학회지 Vol.23 No.3
Aspergillus niger biomass, an industrial by-product of citric acid fermentation is an emergent source of glycoderivatives with applications in biofuel, cosmetics, feed, energy, food, medicine, and nanotechnology. In this study, the effect of purified neutral protease for deprotenization of fungal biomass studied at various levels (0, 5, 10, 20 and 40 U/100 mg of biomass) and the saccharification of fungal biomass was evaluated with amylolytic enzymes and chitosanases. The efficiency of deproteinization of fungal biomass was based on the enzyme concentration and contact time. Protease at a concentration of 20 U/100 mg of dry biomass and with a contact time of 8 h achieved 30% final deproteinization. No effect on saccharification of A. niger biomass was observed by treatment with purified amylolytic enzymes. Meanwhile, the endo- and exo-chitosanases treatment yielded 54 g of g reducing sugars (equivalent to amino sugars)/ kg of fungal biomass, which can be employed for tailor-made carbohydrate production.
Luz M. Ramos-Ponce,Mireille Vega,Edith Colunga-Urbina,Georgina C. Sandoval-Fabián,Nagamani Balagurusamy,Juan Carlos Contreras-Esquivel,Francisco J. Rodriguez-Gonzalez 한국식품과학회 2010 Food Science and Biotechnology Vol.19 No.3
A colorimetric method for quantitative measurement of free amino groups of water soluble chitin derivatives is described. The method utilizes genipin as a natural and specific reagent for determining the concentration of free amino groups in samples of water soluble chitin derivatives. The blue color adduct (complex) formed during genipin reaction with free amino groups was measured at about 589 nm and Beer-Lambert’s law obeyed over the concentration range of 50 to 300 mg/L. Parameters of analytical conditions were considered and kept constant during the experimental procedure. Highly acetylated water soluble chitin derivatives can be differentiated from water soluble chitosan using this genipin method. The colorimetric method with genipin was proved to be a rapid and efficient technique to determine the free amino groups in water soluble chitin derivatives. This method can also be applied for the detection of the enzymatic activity of chitindeacetylase.
Screening of Industrial Enzymes for Deproteinization of Shrimp Head for Chitin Recovery
Angel U. Valdez-Peña,Adriana Hernandez-Rivera,Iliana M. De-la-Garza-Rodriguez,Judith D. Espinoza-Perez,Georgina C. Sandoval-Fabian,Nagamani Balagurusamy,Juan Carlos Contreras-Esquivel 한국식품과학회 2010 Food Science and Biotechnology Vol.19 No.2
Food grade proteolytic enzymes were examined for deproteinization of shrimp head. Shrimp head was easily deproteinized by Alcalase® and trypsin at a pH of 8.0. Alcalase was chosen as the most efficient commercial enzyme for deproteinization of shrimp head. Alcalase treatment of shrimp head recorded 61% of weight loss on dry basis and a residual protein of 275 mg/g dried shrimp head. The enzymatically deproteinized shrimp head was later demineralized with lactic acid using microwave radiation at 400W. The combination of enzymatic and physicochemical treatments promoted the chitin recovery from dried shrimp head under eco-friendly conditions.