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Pectin from Passion Fruit Fiber and Its Modification by Pectinmethylesterase
Contreras-Esquivel, Juan Carlos,Aguilar, Cristobal N.,Montanez, Julio C.,Brandelli, Adriano,Espinoza-Perez, Judith D.,Renard, Catherine M.G.C. The Korean Society of Food Science and Nutrition 2010 Preventive Nutrition and Food Science Vol.15 No.1
Passion fruit fiber pectin gels represent a new alternative pectin source with potential for food and non-food applications on a commercial scale. Pectic polysaccharides were extracted from passion fruit (Passiflora edulis) fiber using citric acid as a clean catalyst and autoclaved for 20 to 60 min at $121^{\circ}C$. The best condition of pectin yield with the highest molecular weight was obtained with 1.0% of citric acid (250 mg/g dry passion fruit fiber pectin) for 20 min of autoclaving. Spectroscopic analyses by Fourier transform infrared, enzymatic degradation reactions, and ion-exchange chromatography assays showed that passion fruit pectin extracted for 20 min was homogeneous high methoxylated pectin (70%). Gel permeation analysis confirmed that the pectin extract obtained by autoclaving by 20 min showed higher molecular weights than those autoclaved for 40 and 60 min. Passion fruit pectin extracted for 20 min was enzymatically modified with fungal pectinmethylesterase to create restructured gels. Short autoclave treatment (20 min) with citric acid as extractant resulted in a significant increase of gel strength, improving pectin extraction in terms of functionality. The treatment of solubilized material (pectic polysaccharides) in the presence of insoluble material (cellulose and hemicellulose) with pectinmethylesterase and calcium led to the creation of a stiffer passion fruit fiber pectin gel, while syneresis was not observed.
Pectin from Passion Fruit Fiber and Its Modification by Pectinmethylesterase
Juan Carlos Contreras-Esquivel,Cristobal N. Aguilar,Julio C. Montanez,Adriano Brandelli,Judith D. Espinoza-Perez,Catherine M.G.C. Renard 한국식품영양과학회 2010 Preventive Nutrition and Food Science Vol.15 No.1
Passion fruit fiber pectin gels represent a new alternative pectin source with potential for food and non-food applications on a commercial scale. Pectic polysaccharides were extracted from passion fruit (Passiflora edulis) fiber using citric acid as a clean catalyst and autoclaved for 20 to 60 min at 121℃. The best condition of pectin yield with the highest molecular weight was obtained with 1.0% of citric acid (250 ㎎/g dry passion fruit fiber pectin) for 20 min of autoclaving. Spectroscopic analyses by Fourier transform infrared, enzymatic degradation reactions, and ion-exchange chromatography assays showed that passion fruit pectin extracted for 20 min was homogeneous high methoxylated pectin (70%). Gel permeation analysis confirmed that the pectin extract obtained by autoclaving by 20 min showed higher molecular weights than those autoclaved for 40 and 60 min. Passion fruit pectin extracted for 20 min was enzymatically modified with fungal pectinmethylesterase to create restructured gels. Short autoclave treatment (20 min) with citric acid as extractant resulted in a significant increase of gel strength, improving pectin extraction in terms of functionality. The treatment of solubilized material (pectic polysaccharides) in the presence of insoluble material (cellulose and hemicellulose) with pectinmethylesterase and calcium led to the creation of a stiffer passion fruit fiber pectin gel, while syneresis was not observed.
Optimization of Tannase Production by Aspergillus niger in Solid-State Packed-Bed Bioreactor
( Rodriguez Duran Luis ),( Juan C. Contreras Esquivel ),( Raul Rodriguez ),( L. Arely Prado Barragan ),( Cristobal N. Aguilar ) 한국미생물 · 생명공학회 2011 Journal of microbiology and biotechnology Vol.21 No.9
Tannin acyl hydrolase, also known as tannase, is an enzyme with important applications in the food, feed, pharmaceutical, and chemical industries. However, despite a growing interest in the catalytic properties of tannase, its practical use is very limited owing to high production costs. Several studies have already demonstrated the advantages of solid-state fermentation (SSF) for the production of fungal tannase, yet the optimal conditions for enzyme production strongly depend on the microbial strain utilized. Therefore, the aim of this study was to improve the tannase production by a locally isolated A. niger strain in an SSF system. The SSF was carried out in packed-bed bioreactors using polyurethane foam as an inert support impregnated with defined culture media. The process parameters influencing the enzyme production were identified using a Plackett-Burman design, where the substrate concentration, initial pH, and incubation temperature were determined as the most significant. These parameters were then further optimized using a Box-Behnken design. The maximum tannase production was obtained with a high tannic acid concentration (50 g/l), relatively low incubation temperature (30oC), and unique low initial pH (4.0). The statistical strategy aided in increasing the enzyme activity nearly 1.97-fold, from 4,030 to 7,955 U/l. Consequently, these findings can lead to the development of a fermentation system that is able to produce large amounts of tannase in economical, compact, and scalable reactors.
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.