[Application of bionic technology to speciation analysis and bioavailability assessment of nickel in transgenic soybean].

The safety of transgenic food has been paid the most attention to by the public and scientists. Trace metal bioavailability could provide information for safety assessment of transgenic food. The critical functional digestion and absorption in the gastrointestinal tract were simulated by bionic gastrointestinal digestion, metabolism of gut microbiota, and bionic biomembrane adsorption with liposome and then used for the pretreatment of transgenic and general soybeans.

The genetically modified suilysin, rSLY(P353L), provides a candidate vaccine that suppresses proinflammatory response and reduces fatality following infection with Streptococcus suis.

Streptococcus suis is a persistent global hazard in the swine industry and an emerging threat to public health. The high mortality in China following outbreaks of streptococcal toxic shock syndrome (STSS) underscores the urgency for effective prevention. A limited understanding of the pathogenesis of S.

Circular permutation provides an evolutionary link between two families of calcium-dependent carbohydrate binding modules.

The microbial deconstruction of the plant cell wall is a critical biological process, which also provides important substrates for environmentally sustainable industries. Enzymes that hydrolyze the plant cell wall generally contain non-catalytic carbohydrate binding modules (CBMs) that contribute to plant cell wall degradation. Here we report the biochemical properties and crystal structure of a family of CBMs (CBM60) that are located in xylanases.

Probing the structural basis for the difference in thermostability displayed by family 10 xylanases.

Thermostability is an important property of industrially significant hydrolytic enzymes: understanding the structural basis for this attribute will underpin the future biotechnological exploitation of these biocatalysts. The Cellvibrio family 10 (GH10) xylanases display considerable sequence identity but exhibit significant differences in thermostability; thus, these enzymes represent excellent models to examine the structural basis for the variation in stability displayed by these glycoside hydrolases. Here, we have subjected the intracellular Cellvibrio mixtus xylanase CmXyn10B to forced protein evolution.

X4 modules represent a new family of carbohydrate-binding modules that display novel properties.

The hydrolysis of the plant cell wall by microbial glycoside hydrolases and esterases is the primary mechanism by which stored organic carbon is utilized in the biosphere, and thus these enzymes are of considerable biological and industrial importance. Plant cell wall-degrading enzymes in general display a modular architecture comprising catalytic and non-catalytic modules. The X4 modules in glycoside hydrolases represent a large family of non-catalytic modules whose function is unknown.

Structural and biochemical analysis of Cellvibrio japonicus xylanase 10C: how variation in substrate-binding cleft influences the catalytic profile of family GH-10 xylanases.

Microbial degradation of the plant cell wall is the primary mechanism by which carbon is utilized in the biosphere. The hydrolysis of xylan, by endo-beta-1,4-xylanases (xylanases), is one of the key reactions in this process. Although amino acid sequence variations are evident in the substrate binding cleft of "family GH10" xylanases (see afmb.