• Geomechanics and Engineering
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• v.17 no.4
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• pp.333-342
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• 2019

Geological dynamic hazards during coal mining can be caused by the failure of a composite system consisting of roof rock and coal layers, subject to different loading rates due to different advancing velocities in the working face. In this paper, the uniaxial compression test simulations on the composite rock-coal layers were performed using $PFC^{2D}$ software and especially the effects of loading rate on the stress-strain behavior, strength characteristics and crack nucleation, propagation and coalescence in a composite layer were analyzed. In addition, considering the composite layer, the mechanisms for the advanced bore decompression in coal to prevent the geological dynamic hazards at a rapid advancing velocity of working face were explored. The uniaxial compressive strength and peak strain are found to increase with the increase of loading rate. After post-peak point, the stress-strain curve shows a steep stepped drop at a low loading rate, while the stress-strain curve exhibits a slowly progressive decrease at a high loading rate. The cracking mainly occurs within coal, and no apparent cracking is observed for rock. While at a high loading rate, the rock near the bedding plane is damaged by rapid crack propagation in coal. The cracking pattern is not a single shear zone, but exhibits as two simultaneously propagating shear zones in a "X" shape. Following this, the coal breaks into many pieces and the fragment size and number increase with loading rate. Whereas a low loading rate promotes the development of tensile crack, the failure pattern shows a V-shaped hybrid shear and tensile failure. The shear failure becomes dominant with an increasing loading rate. Meanwhile, with the increase of loading rate, the width of the main shear failure zone increases. Moreover, the advanced bore decompression changes the physical property and energy accumulation conditions of the composite layer, which increases the strain energy dissipation, and the occurrence possibility of geological dynamic hazards is reduced at a rapid advancing velocity of working face.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 2001.06a
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• pp.40-45
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• 2001

Raw starch-digesting amylase (BF-2A, M.W. 93, 000 Da) from Bacillus circulans F-2 was converted to two components during digestion with subtilisin. Two components were separated and designated as BF-2A' (63, 000 Da) and BF-2B (30, 000 Da), respectively. BF-2A' exhibited the same hydrolysis curve for soluble starch as the original amylase (BF-2A). Moreover, the catalytic activities of original and modified enzymes were indistinguishable in $K_{m}$, Vmax for, and in their specific activity for soluble starch hydrolysis. However, its adsorbability and digestibility on raw starch was greatly decreased. Furthermore, the enzymatic action pattern on soluble starch was greatly different from that of the BF-2A. A smaller peptide (BF-2B) showed adsorb ability onto raw starch. By these results, it is suggested that the larger peptide (BF-2A') has a region responsible for the expression of the enzyme activity to hydrolyze soluble substrate, and the smaller peptide (BF-2B) plays a role on raw starch adsorption. A similar phenomenon is observed during limited proteinase K, thermolysin, and endopeptidase Glu-C proteolysis of the enzyme. Fragments resulting from proteolysis were characterized by immunoblotting with anti-RSDA. The proteolytic patterns resulting from proteinase K and subtilisin were the same, producing 63- and 30-kDa fragments. Similar patterns were obtained with endopeptidase Glu-C or thermolysin. All proteolytic digests contained a common, major 63-kDa fragment. Inactivation of RSDA activity results from splitting off the C-terminal domain. Hence, it seems probable that the protease sensitive locus is in a hinge region susceptible to cleavage. Extracellular enzymes immunoreactive toward anti-RSDA were detected through whole bacterial cultivation. Proteins of sizes 93-, 75-, 63-, 55-, 38-, and 31-kDa were immunologically identical to RSDA. Of these, the 75-kDa and 63-kDa proteins correspond to the major products of proteolysis with Glu-C and thermolysin. These results postulated that enzyme heterogeneity of the raw starch-hydrolysis system might arise from the endogeneous proteolytic activity of the bacterium. Truncated forms of rsda, in which the gene sequence encoding the conserved domain had been deleted, directed the synthesis of a functional amylase that did not bind to raw starch. This indicates that the conserved region of RSDA constitutes a raw starch-binding domain, which is distinct from the active centre. The possible role of this substrate-binding region is discussed.d.