Cellobiohydrolase I from Trichoderma longibrachiatum)

• Description:

  Cellobiohydrolase I from Trichoderma longibrachiatum) _x000D_ Catalog number: B2014927_x000D_ Lot number: Batch Dependent_x000D_ Expiration Date: Batch dependent_x000D_ Amount: 5 Units_x000D_ Molecular Weight or Concentration: 65 kDa_x000D_ Supplied as: Suspension_x000D_ Applications: molecular tool for various biochemical applications_x000D_ Storage: 2-8oC_x000D_ Keywords: cellulose 1,4-beta-cellobiosidase (non-reducing end); 4-beta-D-glucan cellobiohydrolase_x000D_ Grade: Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um._x000D_ _x000D_ References:_x000D_ 1: Gusakov AV, Protas OV, Chernoglazov VM, Sinitsyn AP, Kovalysheva GV, Shpanchenko OV, Ermolova OV. Transglycosylation activity of cellobiohydrolase I from Trichoderma longibrachiatum on synthetic and natural substrates Biochim Biophys Acta. 1991 Apr 9;1073(3):481-5._x000D_ 2: Zhang Y, Wang Y, Yang J, Yang W, Wang X, Wu C, Song Y. Improved γ-Linolenic Acid Production from Cellulose in Mucor circinelloides via Coexpression of Cellobiohydrolase and Delta-6 Desaturase J Agric Food Chem. 2022 Apr 13;70(14):4373-4381._x000D_ 3: Fox JM, Levine SE, Clark DS, Blanch HW. Initial- and processive-cut products reveal cellobiohydrolase rate limitations and the role of companion enzymes Biochemistry. 2012 Jan 10;51(1):442-52._x000D_ 4: Tokuyasu K, Tabuse M, Miyamoto M, Matsuki J, Yoza K. Pretreatment of microcrystalline cellulose flakes with CaCl2 increases the surface area, and thus improves enzymatic saccharification Carbohydr Res. 2008 May 19;343(7):1232-6._x000D_ 5: Maurer SA, Brady NW, Fajardo NP, Radke CJ. Surface kinetics for cooperative fungal cellulase digestion of cellulose from quartz crystal microgravimetry J Colloid Interface Sci. 2013 Mar 15;394:498-508._x000D_ 6: Morgavi DP, Beauchemin KA, Nsereko VL, Rode LM, McAllister TA, Iwaasa AD, Wang Y, Yang WZ. Resistance of feed enzymes to proteolytic inactivation by rumen microorganisms and gastrointestinal proteases J Anim Sci. 2001 Jun;79(6):1621-30._x000D_ 7: Pramanik S, Semenova MV, M Rozhkova A, Zorov IN, Korotkova O, Sinitsyn AP, Davari MD. An engineered cellobiohydrolase I for sustainable degradation of lignocellulosic biomass Biotechnol Bioeng. 2021 Oct;118(10):4014-4027._x000D_ 8: Dos Santos FC, de Oliveira MAS, Seixas FAV, Barbosa-Tessmann IP. A Novel Cellobiohydrolase I (CBHI) from Penicillium digitatum: Production, Purification, and Characterization Appl Biochem Biotechnol. 2020 Sep;192(1):257-282._x000D_ 9: Westh P, Borch K, Sørensen T, Tokin R, Kari J, Badino S, Cavaleiro MA, Røjel N, Christensen S, Vesterager CS, Schiano-di-Cola C. Thermoactivation of a cellobiohydrolase Biotechnol Bioeng. 2018 Apr;115(4):831-838._x000D_ 10: Xin D, Ge X, Sun Z, Viikari L, Zhang J. Competitive inhibition of cellobiohydrolase I by manno-oligosaccharides Enzyme Microb Technol. 2015 Jan;68:62-8. _x000D_ _x000D_ Products Related to Cellobiohydrolase I from Trichoderma longibrachiatum) can be found at Enzymes

• Short Description:

  Catalog Number: B2014927 (5 Units)_x000D_ Cellobiohydrolase I from Trichoderma longibrachiatum) is a high quality Cellobiohydrolase I (Trichoderma longibrachiatum). This product has been used as molecular tool for various biochemical applications. It has also been used in a wide array of other chemical and immunological applications. Custom bulk amounts of this product are available upon request._x000D_ _x000D_

• Weight:

  0.15

• Length:

  2

• Width:

  0.5

• Height :

  0.5