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49694-21-5

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49694-21-5 Usage

Uses

Xylohexaose is a xylose oligomer that is of interest to many fields of study and is an intermediate reaction product of the hydrolysis of hemicelluloses.

Reactions

Most of the chemical and biochemical processes used for the de-polymerization of structural polymers of lignocellulosic biomass are environment unfriendly and costly. Here an efficient process based on xylanase, produced by Acinetobacter pittii MASK25 (MTCC 25132), hydrolysis of only physically treated rice straw and corn cob has been developed for the production of xylooligosaccharides. Bacterial strain isolated from soil was found to produce maximum xylanase at 30 °C and pH 7. While the optimum temperature and pH of xylanase were characterized as 40 °C and 5. Process was further improved by developing magnetic-xylanase CLEA. Crude xylanase and magnetic-xylanase CLEA could convert respectively more than 45percent and 60percent xylan of the powdered rice straw and corn cob into xylooligosaccharides. Interestingly, hydrolysis by both types of enzymatic forms was found to produce predominantly xylopentose and xylohexose. Hence, the process is environment friendly and the predominant production of xylopentose and xylohexose could find unique prebiotic applications.

Check Digit Verification of cas no

The CAS Registry Mumber 49694-21-5 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 4,9,6,9 and 4 respectively; the second part has 2 digits, 2 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 49694-21:
(7*4)+(6*9)+(5*6)+(4*9)+(3*4)+(2*2)+(1*1)=165
165 % 10 = 5
So 49694-21-5 is a valid CAS Registry Number.

49694-21-5Upstream product

49694-21-5Relevant articles and documents

Molecular cloning and characterization of a novel thermostable xylanase from Paenibacillus campinasensis BL11

Ko, Chun-Han,Tsai, Chung-Hung,Tu, Jenn,Lee, Hang-Yi,Ku, Lan-Ting,Kuo, Pei-An,Lai, Yiu-Kay

supporting information; experimental part, p. 1638 - 1644 (2011/12/03)

An open reading frame (XylX) with 1131 nucleotides from Paenibacillus campinasensis BL11 was cloned and expressed in E. coli. It encodes a family 11 endoxylanase, designated as XylX, of 41kDa. The homology of the amino acid sequence deduced from XylX is only 73% identical to the next closest sequence. XylX contains a family 11 catalytic domain of the glycoside hydrolase and a family 6 cellulose-binding module. The recombinant xylanase was fused to a His-tag for affinity purification. The XylX activity was 2392IU/mg, with a Km of 6.78mg/ml and a Vmax of 4953mol/min/mg under optimal conditions (pH 7, 60°C). At pH 11, 60°C, the activity was still as high as 517IU/mg. Xylanase activities at 60°C under pH 5 to pH 9 remained at more than 69.4% of the initial activity level for 8h. The addition of Hg2+ at 5mM almost completely inhibited xylanase activity, whereas the addition of tris-(2-carboxyethyl)-phosphine (TCEP) and 2-mercaptoethanol stimulated xylanase activity. No relative activities for Avicel, CMC and d-(+)-cellobiose were found. Xylotriose constitutes the majority of the hydrolyzed products from oat spelt and birchwood xylan. Broad pH and temperature stability shows its application potentials for biomass conversion, food and pulp/paper industries.

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