ABSTRACT
BACKGROUND: LXYL-P1-2 is the first reported glycoside hydrolase that can catalyze the transformation of 7-b-xylosyl-10-deacetyltaxol (XDT) to 10-deacetyltaxol (DT) by removing the D-xylosyl group at the C7 position. Successful synthesis of paclitaxel by one-pot method combining the LXYL-P1-2 and 10- deacetylbaccatin III-10-b-O-acetyltransferase (DBAT) using XDT as a precursor, making LXYL-P1-2 a highly promising enzyme for the industrial production of paclitaxel. The aim of this study was to investigate the catalytic potential of LXYL-P1-2 stabilized on magnetic nanoparticles, the surface of which was modified by Ni2+-immobilized cross-linked Fe3O4@Histidine. RESULTS: The diameter of matrix was 2040 nm. The Km value of the immobilized LXYL-P1-2 catalyzing XDT (0.145 mM) was lower than that of the free enzyme (0.452 mM), and the kcat/Km value of immobilized enzyme (12.952 mM s 1 ) was higher than the free form (8.622 mM s 1 ). The immobilized form maintained 50% of its original activity after 15 cycles of reuse. In addition, the stability of immobilized LXYL-P1-2, maintained 84.67% of its initial activity, improved in comparison with free form after 30 d storage at 4 C. CONCLUSIONS: This investigation not only provides an effective procedure for biocatalytic production of DT, but also gives an insight into the application of magnetic material immobilization technology.
Subject(s)
Paclitaxel/biosynthesis , Glycoside Hydrolases/metabolism , Kinetics , Enzymes, Immobilized , Nanoparticles , MagnetsABSTRACT
A massive variety of microorganisms live in and on the human body, especially at oral, skin, vaginal, gastroin-testinal, and respiratory sites. The complicated metabolic activities of microorganisms assist human digestive function and participate in a series of physiological and pathogenetic processes. Carbohydrate-active enzymes (CAZymes) are a series of enzymes that function in degradation, modification, and formation of glycoside bonds. Microbes regulate the physiological and pathogenetic processes of human body by producing various CAZymes to degrade and modify complex carbohydrates and generate signal molecules for further utilization in human cells. Here, we reviewed the mechanisms of complex carbohy-drate metabolism and related microbial CAZymes, especially in digestive tract and oral cavity. We also summarized the rela-tionship between microbial CAZymes and human health, and proposed potential applications.
Subject(s)
Humans , Carbohydrates , Gastrointestinal Tract , MicrobiotaABSTRACT
References and our previous experiment showed that the contents of glycosides were significantly decreased，while the contents of aglycones were significantly increased after processing of Cassiae Semen.It may be related to its glycosidases or the heating process. In order to investigate the reasons, high performance liquid chromatographic (HPLC) was used to study the effects of these two factors on contents of Cassiae Semen's main chemical components in processing. The results showed that glycoside hydrolases was present in Cassiae Semen and could rapidly hydrolyze glycosides from Cassiae Semen into aglycones in suitable temperature with sufficient water.However，it didn't show effect on contents change of main constituents in the procedure of Cassiae Semen processing.The reason for content decrease of glycosides and content increase of aglycones in processed Cassiae Semen was glycoside bond cracking to produce corresponding aglycone at high temperature.This study further provides basis for further revealing of the processing mechanism of Cassiae Semen.
ABSTRACT
ABSTRACT Here, we show the draft genome sequence of Streptomyces sp. F1, a strain isolated from soil with great potential for secretion of hydrolytic enzymes used to deconstruct cellulosic biomass. The draft genome assembly of Streptomyces sp. strain F1 has 69 contigs with a total genome size of 8,142,296 bp and G + C 72.65%. Preliminary genome analysis identified 175 proteins as Carbohydrate-Active Enzymes, being 85 glycoside hydrolases organized in 33 distinct families. This draft genome information provides new insights on the key genes encoding hydrolytic enzymes involved in biomass deconstruction employed by soil bacteria.
Subject(s)
Bacterial Proteins/genetics , Genome, Bacterial , Glycoside Hydrolases/genetics , Soil Microbiology , Streptomyces/enzymology , Streptomyces/isolation & purification , Bacterial Proteins/metabolism , Base Composition , Brazil , Glycoside Hydrolases/metabolism , Multigene Family , Phylogeny , Streptomyces/classification , Streptomyces/geneticsABSTRACT
Heparanase (Hpa) is the only β-D-glucuronidase of degading heparan sulfate proteoglycans in the body of mammalian.Studies have confirmed that Hpa accelerates angiogenesis in multiple physiopathological processes; however there are still a few studies about the expression and role of Hpa after cerebral ischemia.This article mainly introduces the relation between Hpa and angiogenesis after cerebral ischemia.