• Journal of the Korean Society for Precision Engineering
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• v.28 no.7
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• pp.821-826
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• 2011

This paper deals with an analysis of dynamic mechanism for the industrial two-step folding automatic door. A nonlinear equation of motion was derived in terms of folding angle to estimate driving forces. Based on this dynamic behavior, time taken during the door's opening well as their velocities were controlled so that the operating conditions can be obtained for the purpose of design. The stiffness of twisting spring was also investigated when the automatic door closed, because a dangerous accident takes place from the door's free falling. The current research will be a very useful tool in the near future for the dynamic analysis for the multi-step folding automatic door.

• Journal of the Korean Society of Manufacturing Process Engineers
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• v.10 no.4
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• pp.16-21
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• 2011

This paper described an analysis of dynamic mechanism for the industrial two-step folding automatic door using commercial software packages. Two modeling types of operating on the guide rail, the sliding one and the rolling, were adopted to investigate effects of impact force when the door ascends the guide rail. The magnitude of impact force was found very peaklike large over an initial duration of the door's moving up. The amount of damping coefficient for alleviating this shock was controlled to such a moderate degree that the operating conditions can be obtained for the purpose of design. Moreover the behavior of both dynamic stress and deformation were observed for acquirement of structural reliabilities of the combined guide rail and rolling mechanism. This research will be a very useful tool in the near future for the dynamic analysis of the multi-step folding automatic door.

• Proceedings of the Microbiological Society of Korea Conference
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• 2001.11a
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• pp.16-25
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• 2001

A genomic library of biphenyl-degrading strain Comamonas sp. SMN4 was constructed by using the cosmid vector pWE15 and introduced into Escherichia coli. Of 1,000 recombinant clones tested, two clones that expressed 2,3-dihydroxybiphenyl 1,2-dioxygenase activity were found (named pNB 1 and pNB2). From pNB1 clone, subclone pNA210, demonstrated 2,3-dihydroxybiphenyl 1,2-dioxygenase activity, is isolated. 2,3-Dihydroxybiphenyl 1,2-dioxygenase (23DBDO, BphC) is an extradiol-type dioxygenase that involved in third step of biphenyl degradation pathway. The nucleotide sequence of the Comamonas sp. SMN4 gene bphC, which encodes 23DBDO, was cloned into a plasmid pQE30. The His-tagged 23DBDO produced by a recombinant Escherichia coli, SG 13009 (pREP4)(pNPC), and purified with a Ni-nitrilotriacetic acid resin affinity column using the His-bind Qiagen system. The His-tagged 23DBDO construction was active. SDS-PAGE analysis of the purified active 23DBDO gave a single band of 32 kDa; this is in agreement with the size of the bphC coding region. The 23DBDO exhibited maximum activity at pH 9.0. The CD data for the pHs, showed that this enzyme had a typical a-helical folding structures at neutral pHs ranged from pH 4.5 to pH 9.0. This structure maintained up to pH 10.5. However, this high stable folding strucure was converted to unfolded structure in acidic region (pH 2.5) or in high pH (pH 12.0). The result of CD spectra observed with pH effects on 23DBDO activity, suggested that charge transition by pH change have affected change of conformational structure for 23DBDO catalytic reaction. The $K_m$ for 2,3-dihydroxybiphenyl, 3-metylcatechol, 4-methylcatechol and catechol was 11.7 $\mu$M, 24 $\mu$M, 50 mM and 625 $\mu$M.