World Library  


Add to Book Shelf
Flag as Inappropriate
Email this Book

Plos One : Purification, Gene Cloning, and Biochemical Characterization of a Β-glucosidase Capable of Hydrolyzing Sesaminol Triglucoside from Paenibacillus Sp. Kb0549, Volume 8

By Raaij, J. Van, Mark

Click here to view

Book Id: WPLBN0003965488
Format Type: PDF eBook :
File Size:
Reproduction Date: 2015

Title: Plos One : Purification, Gene Cloning, and Biochemical Characterization of a Β-glucosidase Capable of Hydrolyzing Sesaminol Triglucoside from Paenibacillus Sp. Kb0549, Volume 8  
Author: Raaij, J. Van, Mark
Volume: Volume 8
Language: English
Subject: Journals, Science, Medical Science
Collections: Periodicals: Journal and Magazine Collection (Contemporary)
Historic
Publication Date:
Publisher: Plos

Citation

APA MLA Chicago

Mark Raaij, J. V. (n.d.). Plos One : Purification, Gene Cloning, and Biochemical Characterization of a Β-glucosidase Capable of Hydrolyzing Sesaminol Triglucoside from Paenibacillus Sp. Kb0549, Volume 8. Retrieved from http://netlibrary.net/


Description
Description : The triglucoside of sesaminol, i.e., 2,6-O-di(b-D-glucopyranosyl)-b-D- glucopyranosylsesaminol (STG), occurs abundantly in sesame seeds and sesame oil cake and serves as an inexpensive source for the industrial production of sesaminol, an antioxidant that displays a number of bioactivities beneficial to human health. However, STG has been shown to be highly resistant to the action of b-glucosidases, in part due to its branched-chain glycon structure, and these circumstances hampered the efficient utilization of STG. We found that a strain (KB0549) of the genus Paenibacillus produced a novel enzyme capable of efficiently hydrolyzing STG. This enzyme, termed PSTG, was a tetrameric protein consisting of identical subunits with an approximate molecular mass of 80 kDa. The PSTG gene was cloned on the basis of the partial amino acid sequences of the purified enzyme. Sequence comparison showed that the enzyme belonged to the glycoside hydrolase family 3, with significant similarities to the Paenibacillus glucocerebrosidase (63% identity) and to Bgl3B of Thermotoga neapolitana (37% identity). The recombinant enzyme (rPSTG) was highly specific for b-glucosidic linkage, and kcat and kcat/ Km values for the rPSTG-catalyzed hydrolysis of p-nitrophenyl-b-glucopyraniside at 37uC and pH 6.5 were 44 s21 and 426 s21 mM21, respectively. The specificity analyses also revealed that the enzyme acted more efficiently on sophorose than on cellobiose and gentiobiose. Thus, rPSTG is the first example of a b-glucosidase with higher reactivity for b-1,2- glucosidic linkage than for b-1,4- and b-1,6-glucosidic linkages, as far as could be ascertained. This unique specificity is, at least in part, responsible for the enzyme’s ability to efficiently decompose STG.

 

Click To View

Additional Books


  • Plos One : Supplementing with Non-glycos... (by )
  • Plos One : Evaluation of Estrogenic Acti... (by )
  • Plos One : Type-specific Cell Line Model... (by )
  • Plos One : Mir-206 Represses Hypertrophy... (by )
  • Plos One : Linking Protective Gab2Varian... (by )
  • Plos One : Application of On-line Nanolc... (by )
  • Plos One : Impact of Metabolic Syndrome ... (by )
  • Plos One : Possible Association Between ... (by )
  • Plos One : Renin-angiotensin System Bloc... (by )
  • Plos One : Corneal Absorption of a New R... (by )
  • Plos One : Impact of Genetic Polymorphis... (by )
  • Plos One : Just One Position-independent... (by )
Scroll Left
Scroll Right

 



Copyright © World Library Foundation. All rights reserved. eBooks from World Library are sponsored by the World Library Foundation,
a 501c(4) Member's Support Non-Profit Organization, and is NOT affiliated with any governmental agency or department.