¥°¥ú¬ì§Þ¤j¾Ç ±Ð®v­Ó¤Hºô¯¸
 

 

 

 
³Ì«á§ó·s®É¶¡¡G107/05/21 11:37:22
­Ó¤HÀÉ®×
* ±Ð®v°ò¥»¸ê®Æ
 
©m¦W¡Gù¿·ªâ
¾ºÙ¡G±Ð±Â
±M­Ý¥ô§O¡G±M¥ô±Ð®v
¸u¥ô¨t©Ò¡G­¹«~¬ì§Þ¨t(©Ò)
E-mail: hflo@sunrise.hk.edu.tw
E-Portfolio¡G¶}±Ò³sµ²
Office hours¡G¬P´Á¤G¡G²Ä4-¤¤¤È¸`¡F¬P´Á¤T¡G²Ä4-¤¤¤È¸`¡F¬P´Á¥|¡G²Ä5-6¸`
1062 ¾Ç´Á±Â½Ò½Òµ{¡G¤ÀªR¤Æ¾Ç¹êÅç¡B­¹«~¥Íª«§Þ³N¹êÅç¡B­¹«~¥Íª«§Þ³N
¦æ¬F¾¡GµL

* ¾Ç¾ú»P¸g¾ú

¾Ç¾ú¡G
ÀR©y¤j¾Ç­¹«~Àç¾i¨tÀç¾i¥Í¤Æ²Õ³Õ¤h
ÀR©y¤k¤l¤å²z¾Ç°|À³¥Î¤Æ¾Ç¨t¾Ç¤h
 
¸g¾ú¡G
ÃÒ·Ó¡G
¤º¬F³¡¤Æ¾Ç(¤A¯Å)
¦æ¬F°|³Ò¤u©e­û·|§Þ³N¤h§Þ¯àÀË©w³N¬ì´ú¸ÕºÊµû¤H­ûÃÒ®Ñ-­¹«~ÀËÅç¤ÀªR¾Ãþ¤A¡B¤þ¯Å
¦æ¬F°|³Ò¤u©e­û·|­¹«~ÀËÅç¤ÀªR(¤A¯Å)
* Àò¹{¼ú¶µ»PºaÅA¸ê®Æ
* ´Á¥Z½×¤å
1060812²Ä¤G§@ªÌ Application of Bacillus licheniformis £^-glutamyltranspeptidase to the biocatalytic synthesis of £^-glutamyl-phenylalanine Biocatalysis and Agricultural Biotechnology SCI
1041229²Ä¤@§@ªÌ Gene expression and molecular characterization of a chaperoneprotein HtpG from Bacillus licheniformis. International Journal of Biological Macromolecules SCI
1040504²Ä¤G§@ªÌ Enzymatic synthesis of £^-L-glutamyl-S-allyl-L- cysteine, a naturallyoccurring organosulfur compound from garlic, by Bacillus licheniformis £^-glutamyltrans peptidase. Enzyme and Microbial Technology SCI
1031022³q°T§@ªÌ Residues Phe103 and Phe149 are critical for the co-chaperone activityof Bacillus licheniformis GrpE International Journal of Biological Macromolecules SCI
1021029²Ä¤T§@ªÌ Biophysical characterization of a recombinant aminopeptidase II from the thermophilic bacterium Bacillus stearothermophilus J Biol Phys SCI
1020301²Ä¤@§@ªÌ Simultaneous Purification and Immobilization of Histidine-tagged Bacillus licheniformis Aldehyde Dehydrogenase on Metal Affinity Magnetic Beads Journal of Pure and Applied Microbiology SCI
1011101²Ä¥|§@ªÌ Characterization of Glycine Substitution Mutations within the Putative NAD+-binding Site of Bacillus licheniformis Aldehyde Dehydrogenase Protein & Peptide Letters SCI
1011025²Ä¤T§@ªÌ Experimental evidence for the involvement of amino acid residue Glu398 in the FEBS Open Bio SCI
1011025²Ä¤T§@ªÌ Introduction of a unique tryptophan residue into various positions of Bacillus licheniformis DnaK International Journal of Biological Macromolecules SCI
1010812³q°T§@ªÌ Sorbitol counteracts temperature- and chemical-induced J Ind Microbiol Biotechnol SCI
1001011³q°T§@ªÌ Contribution of Conserved Glu255 and Cys289 Residues to Catalytic Activity of Recombinant Aldehyde Dehydrogenase from Bacillus licheniformis Biochemistry (Moscow) SCI
1000827²Ä¤@§@ªÌ Biophysical studies of an NAD(P)+-dependent aldehyde dehydrogenase from Bacillus licheniformis Eur Biophys J SCI
1000114²Ä¤­§@ªÌ Biophysical characterization of Bacillus licheniformis and Escherichia coli -glutamyltranspeptidases: A comparative analysis International Journal of Biological Macromolecules SCI
1000101³q°T§@ªÌ Substrate Specificity and Kinetic Characterization of a Recombinant Dipeptidyl Caroxypeptidase from Escherichia coli. Research Journal of Microbiology ¨ä¥L
0990522²Ä¤@§@ªÌ Gene Cloning and Biochemical Characterization of a NAD(P)+-Dependent Aldehyde Dehydrogenase from Bacillus licheniformis. Molecular Biotechnology SCI
0990306²Ä¤T§@ªÌ Mutational analysis of the proposed calcium-binding aspartates of a truncated £\-amylase from Bacillus sp. strain TS-23. Annals of Microbiology SCI
0990301²Ä¤@§@ªÌ Probing the catalytically essential residues of a recombinant dipeptidyl carboxypeptidase from Escherichia coli. Biologia: Section Cellular and Molecular Biology SCI
0981201²Ä¥|§@ªÌ Role of the conserved Thr399 and Thr417 residues of a recombinant Bacillus licheniformis ƒ×-glutamyltranspeptidase as evaluated by mutational analysis. Current Microbiology SCI
0980701²Ä¤@§@ªÌ Cobalt-chelated magnetic particles for one-step purification and immobilization of His6-tagged Escherichia coli ƒ×-glutamyltranspeptidase. Biocatalysis & Biotransfomation SCI
0980520³q°T§@ªÌ Deletion analysis of the C-terminal region of a molecular chaperone DnaK from Bacillus licheniformis. Arch Microbiol SCI
0980301²Ä¤@§@ªÌ Influence of signal-peptide truncations on the functional expression of Escherichia coli £^-glutamyltranspeptidase. Journal of Basic Microbiology SCI
0971101²Ä¤@§@ªÌ The dipeptidyl carboxypeptidase of Escherichia coli novablue: overproduction and molecular characterization of the recombinant enzyme World J Microbiol Biotechnology SCI
0970901²Ä¥|§@ªÌ Influence of N-Terminal Truncations on the Functional Expression of Bacillus licheniformis c-Glutamyltranspeptidase in Recombinant Escherichia coli Current Microbiology SCI
0970601²Ä¤G§@ªÌ Immobilization of Escherichia coli novablue £^-glutamyl -transpeptidase in Ca-alginate-k- carrageenan beads. Applied Biochemistry and Biotechnology SCI
0970601²Ä¤@§@ªÌ Impact of Arg210-Ser211 deletion on thermostability of a truncated Bacillus sp. strain TS-23 a-amylase. Process Biochemistry. Process Biochemistry SCI
0970501²Ä¤@§@ªÌ Glutamic acid 219 is critical for the thermostability of a truncated £\-amylase from alkaliphilic and thermophilic Bacillus sp. strain TS-23. World Journal of Microbiology and Biotechnology SCI
0970201²Ä¤@§@ªÌ Characterization of lysine-tagged Bacillus stearothermophilus leucine aminopeptidase II immobilized onto carboxylated gold nanoparticles. Journal of Molecular Catalysis B: Enzymatic SCI
0970101²Ä¤@§@ªÌ Influence of signal-peptide truncations on the functional expression of Escherichia coli £^-glutamyltranspeptidase. Journal of Basic Microbiology SCI
0960801²Ä¤@§@ªÌ Site-directed mutagenesis of the conserved Thr407, Asp433, and Met464 residues in the small subunit of Escherichia coli £^-glutamyltranspeptidase Indian Journal of Biochemistry & Biophysics SCI
0950320²Ä¤@§@ªÌ Identification of Glutamate Residues Important for Catalytic Activity or Thermostability of a Truncated Bacillus sp. Strain TS-23 £\-amylase by Site-directed Mutagenesis The Protein Journal SCI
0940703²Ä¤T§@ªÌ Adsorption-elution purification of chimeric Bacillus stearothermophilus leucineaminopeptidase II with raw-starch-binding activity. World Journal of Microbiology & Biotechnology SCI
0940603²Ä¤@§@ªÌ Stabilization of a truncated Bacillus sp. strain TS-23 £\-amylase by replacing histidine-436 with aspartate. World Journal of Microbiology & Biotechnology 21:411¡V416 SCI
0930610²Ä¤T§@ªÌ Fusion of Bacillus stearothermophilusleucine aminopeptidase II with the raw-starch-binding domain of Bacillus sp. strain TS-23 a-amylase generates a chimeric enzyme with enhanced thermostability and catalytic activity J Ind Microbiol Biotechnol SCI
0930603²Ä¤G§@ªÌ Functional expression of raw starch-binding domain of Bacillus sp. strain TS-23 a-amylase in recombinant Escherichia coli. Strach/St¡Hrke SCI
0921203²Ä¤G§@ªÌ Identification of essential histidine residues in a recombinant £\-amylase of thermophilic and alkaliphilic Bacillus sp. strain TS-23. Extremophiles SCI
0920403²Ä¤@§@ªÌ Site-directed mutagenesis of the conserved threonine, tryptophan, and lysine residues in the starch-binding domain of Bacillus sp. strain TS-23 £\-amylase Current Microbiology SCI
0920303²Ä¤G§@ªÌ Replacement of methionine 208 in a truncated Bacillus sp. TS-23 £\-amylase with oxidation-resistant leucine enhances its resistance to hydrogen peroxide. Current Microbiology SCI
0910801²Ä¤@§@ªÌ Deletion analysis of the C-terminal region of the £\-amylase of Bacillus sp. strain TS-23. Archives of Microbiology SCI
0910601²Ä¤G§@ªÌ Isolation of a recombinant Bacillus sp. TS-23 ¡H-amylase by adsorption-elution on raw starch. Starch/St¡Hrke SCI
0900601²Ä¤@§@ªÌ The N-terminal signal sequence and the last 98 amino acids are not essential for the secretion of Bacillus sp. TS-23¡H£\-amylase in Escherichia coli. Current Microbiology SCI
0900501²Ä¤@§@ªÌ Enzymic properties of a SDS-resistant Bacillus sp. TS-23 £\-amylase produced by recombinant Escherichia coli. Process Biochemistry SCI
* ¬ã¨s­p¹º
²£¾Ç­pµe®×(¨p¤H¥ø·~©Îªk¤H¾÷ºc¤§®×¥ó)1070201 - 1100131¦@¦P¥D«ù¤H²£«~«O¦s´Á­­¤§´£¤É¡A¨¾»G¾¯µ¥²K¥[ª«¤§¤ÀªR¤Î¬ÛÃö»sµ{§ïµ½¤§¬ã¨s
²£¾Ç­pµe®×(¨p¤H¥ø·~©Îªk¤H¾÷ºc¤§®×¥ó)1061001 - 1070930¦@¦P¥D«ù¤H­×¹¢¾ý¯»¶}µo»P²£«~ÀË´ú¤ÀªR¤§¬ã¨s
²£¾Ç­pµe®×(¨p¤H¥ø·~©Îªk¤H¾÷ºc¤§®×¥ó)1060901 - 1090831¦@¦P¥D«ù¤H­¹«~ÀË´ú¤ÀªR¤§¬ã¨s
²£¾Ç­pµe®×(¨p¤H¥ø·~©Îªk¤H¾÷ºc¤§®×¥ó)1060901 - 1090831¦@¦P¥D«ù¤H­¹«~ÀË´ú¤ÀªR¤§¬ã¨s
²£¾Ç­pµe®×(¨p¤H¥ø·~©Îªk¤H¾÷ºc¤§®×¥ó)1060101 - 1070430¦@¦P¥D«ù¤H»sµ{³W¹º»P«~½è¡B½Ã¥ÍºÞ±±¤§¬ã¨s
²£¾Ç­pµe®×(¨p¤H¥ø·~©Îªk¤H¾÷ºc¤§®×¥ó)1030901 - 1050831¦@¦P¥D«ù¤H103-105¦~«×¹Î¿¯»PBOT­¹§÷½Ã¥Í«~½èºÊ´ú­pµe
²£¾Ç­pµe®×(¨p¤H¥ø·~©Îªk¤H¾÷ºc¤§®×¥ó)1021101 - 1051231¦@¦P¥D«ù¤H­¹§÷¥Íª«©Ê»P¤Æ¾Ç©Ê¦¾¬Vª«ºÊ´ú­pµe
¬ì§Þ³¡®×¥ó(§t±Ð¨|³¡­p¹º)1020801 - 1030731¥D«ù¤H¦a¦çªÞ­M±ìµßîDzæ²B?¤§ÃöÁä´Ý°ò¬ðÅÜ»P¦@»ùÁä©T©w¤Æ
²£¾Ç­pµe®×(¨p¤H¥ø·~©Îªk¤H¾÷ºc¤§®×¥ó)1011220 - 1021231¦@¦P¥D«ù¤H¨§¤z»sµ{§ïµ½»P³W¹º»²¾É
²£¾Ç­pµe®×(¨p¤H¥ø·~©Îªk¤H¾÷ºc¤§®×¥ó)1011101 - 1021130¦@¦P¥D«ù¤H¦M®`¤ÀªR­«ÂIºÞ¨î¨t²Î¤§«Ø¥ßII
²£¾Ç­pµe®×(¨p¤H¥ø·~©Îªk¤H¾÷ºc¤§®×¥ó)1010401 - 1021031¦@¦P¥D«ù¤H²£«~¤ÀªR¤ÎÀËÅç¬ã¨s
²£¾Ç­pµe®×(¨p¤H¥ø·~©Îªk¤H¾÷ºc¤§®×¥ó)1010301 - 1020228¦@¦P¥D«ù¤HÀ\²°«~½è»PÀç¾i¤ÀªR(III)
²£¾Ç­pµe®×(¨p¤H¥ø·~©Îªk¤H¾÷ºc¤§®×¥ó)1001201 - 1011130¦@¦P¥D«ù¤H¦M®`¤ÀªR­«ÂIºÞ¨î¨t²Î¤§«Ø¥ß
²£¾Ç­pµe®×(¨p¤H¥ø·~©Îªk¤H¾÷ºc¤§®×¥ó)1000920 - 1010831¦@¦P¥D«ù¤H¤ô²£«~ÀËÅç­p¹º
²£¾Ç­pµe®×(¨p¤H¥ø·~©Îªk¤H¾÷ºc¤§®×¥ó)1000901 - 1011231¦@¦P¥D«ù¤H»sµ{³W¹º»P²£«~¦w¥þºÊ´ú­p¹º
²£¾Ç­pµe®×(¨p¤H¥ø·~©Îªk¤H¾÷ºc¤§®×¥ó)1000901 - 1011031¦@¦P¥D«ù¤H»sµ{µwÅé³W¹º»PÀËÅç¤ÀªR
¬ì§Þ³¡®×¥ó(§t±Ð¨|³¡­p¹º)1000801 - 1010731¥D«ù¤HBacillus licheniformis¨Ó·½¤§NAD(P)+»²¦]¤l¨Ì¿à«¬îDzæ²B×Q¡G¬¡©Ê»P¨ü½èµ²¦X°Ï°ì´Ý°ò¤§¬ðÅܤÀªR¡B»Ã¯À©T©w¤Æ¥H¤Î§Q¥Î©T©w¤Æ»Ã¯À³B²z¼o¤ô
¬ì§Þ³¡®×¥ó(§t±Ð¨|³¡­p¹º)0990801 - 1000731¥D«ù¤HEscherichia coli k12 µß®è¤§ÂùÐ`?ßn°òÐ`??¤§°ò¦]ªí²{¡B¬ðÅܤÀªR¤ÎÀ³¥Î
¬ì§Þ³¡®×¥ó(§t±Ð¨|³¡­p¹º)0990801 - 1000731¥D«ù¤HEscherichia coli k12 µß®è¤§ÂùÐ`–¦ßn°òÐ`–¦–¡¤§°ò¦]ªí²{¡B¬ðÅܤÀªR¤ÎÀ³¥Î(3/3)
¬ì§Þ³¡®×¥ó(§t±Ð¨|³¡­p¹º)0990801 - 1000731¦@¦P¥D«ù¤HBacillus sp. strain TS-23 alpha-¾ý¯»¡@¤§¼öí©w©Ê§ïµ½¤Î³æ¤@¨BÆJºÏ©Ê²É¤l¯Â¤Æ»P¨ä°t¦X°à°s»Ã¥À¥Í²£°sºë
²£¾Ç­pµe®×(¨p¤H¥ø·~©Îªk¤H¾÷ºc¤§®×¥ó)0990301 - 1010228¦@¦P¥D«ù¤H²°À\«~½è»PÀç¾i¤ÀªR(II)
¬ì§Þ³¡®×¥ó(§t±Ð¨|³¡­p¹º)0980801 - 0990731¥D«ù¤HEscherichia coli¡@k12 µß®è¤§ÂùÐ`?ßn°òÐ`??¤§°ò¦]ªí²{¡B¬ðÅܤÀªR¤ÎÀ³¥Î
¬ì§Þ³¡®×¥ó(§t±Ð¨|³¡­p¹º)0980801 - 0990731¦@¦P¥D«ù¤HBacillus sp. strain TS-23 alpha-¾ý¯»?¤§¼öí©w©Ê§ïµ½¤Î³æ¤@¨BÆJºÏ©Ê²É¤l¯Â¤Æ»P¨ä°t¦X°à°s»Ã¥À¥Í²£°sºë
¬ì§Þ³¡®×¥ó(§t±Ð¨|³¡­p¹º)0970801 - 0980731¥D«ù¤HEscherichia coli¡@k12 µß®è¤§ÂùÐ`?ßn°òÐ`??¤§°ò¦]ªí²{¡B¬ðÅܤÀªR¤ÎÀ³¥Î
¬ì§Þ³¡®×¥ó(§t±Ð¨|³¡­p¹º)0970801 - 1000731¦@¦P¥D«ù¤HBacillus sp. strain TS-23 alpha-¾ý¯»?¤§¼öí©w©Ê§ïµ½¤Î³æ¤@¨BÆJºÏ©Ê²É¤l¯Â¤Æ»P¨ä°t¦X°à°s»Ã¥À¥Í²£°sºë¡@
¬ì§Þ³¡®×¥ó(§t±Ð¨|³¡­p¹º)0960801 - 0970701¥D«ù¤HBacillus licheniformis ßn°òÐ`?¤§°ò¦]ªí²{¡B¥Íª«Âà´«À³¥Î¤Î¬ðÅܤÀªR
¬ì§Þ³¡®×¥ó(§t±Ð¨|³¡­p¹º)0960701 - 0970229¥D«ù¤H¶ÝÆP©Ê°ª·ÅµßBacillus sp. TS-23£\¡V¾ý¯»?Ói°ò»Ä§Ç¦C¤¤°Ï°ìB¤§¬ã¨s»P±´°Q
¬ì§Þ³¡®×¥ó(§t±Ð¨|³¡­p¹º)0950801 - 0960731¥D«ù¤HBacillus sp. TS-23 strain £\-¾ý¯»?219¦ì¸m¤§¾¢Ói»Ä´Ý°òªº¯S©Ê¬ã¨s
 0940801 - 0950731¥D«ù¤HBacillus sp. TS-23 £\-¾ý¯»¡H¤¤436¦ì¸m¤§²Õ´Ói»Ä´Ý°ò¤§¯S©Ê¤ÀªR
 0940801 - 0950731¥D«ù¤HBacillus sp. strain TS-23 a-¯»¾ý¡H¤¤436 ¦ì¸mªº²Õ´®ò»Ä´Ý°ò¤§¯S©Ê¬ã¨s
 0940624 - 0941210¥D«ù¤H´£¤É±Ð®v¹ê°È¯à¤O¤Î¶i­×±M®×­pµe
 0930801 - 0940731¥D«ù¤H Bacillus sp. TS-23 alpha-¾ý¯»¡H¤¤¾¢Ói»Ä´Ý°ò¤§¬ðÅܤÀªR
 0930101 - 0931231¥D«ù¤HBacillus sp. TS-23 alpha-¾ý¯»¡H¥²»Ý²Õ®ò»Ä´Ý°ò¤§¬ðÅܤÀªR
 0920101 - 0921231¥D«ù¤HBacillus sp. TS-23 alpha-¾ý¯»¡H¥Í¾ý¯»§lªþ°Ï°ì¤§¬ã¨s
* ¬ã°Q·|½×¤å
1001202³q°T§@ªÌBacillus licheniformis ¤§NAD(P)+¨Ì¿à«¬îDzæ²B?»Ã¯À©T©w¤Æ¤Î¯S©Ê¬ã¨s¥xÆW­¹«~¬ì§Þ¾Ç·|²Ä41¦¸¦~·|
1000906²Ä¤@§@ªÌBIOPHYSICAL STUDIES OF A NAD(P)+-DEPENDENT ALDEHYDE DEHYDROGENASE FROM BACILLUS LICHENIFORMISIUMS 2011 Sapporo International Union of Microbiological societies 2011 congress
1000616²Ä¤@§@ªÌImmobilization of C-Terminally Lysine-Tagged alpha-Amylase onto Adipic Acid-Modified Magnetic NanoparticlesThe 12th ASEAN FOOD CONFERENCE 2011
0991119³q°T§@ªÌ­°¦åÀ£ÃĪ«captopril¤Î¤j¨§¤ô¸Ñ²G¦hÐ`?¹ïEscherichia coli k-12­«²ÕÂùÐ`?ßn°òÐ`??¤§¼vÅT¥xÆW­¹«~¬ì§Þ¾Ç·|²Ä40¦¸¦~·|
0981127²Ä¤@§@ªÌ¨Ó¦ÛBacillus licheniformis ¤§îDzæ²B?ªº¥Í¤Æ¯S©Ê¤ÀªR¥xÆW­¹«~¬ì§Þ¾Ç·|²Ä39¦¸¦~·|
0981127²Ä¤G§@ªÌ¨Ó¦ÛEscherichia coli k-12¤§­«²ÕÂùÐ`?ßn°òÐ`??(His6-EcDCP)¤§ZnÂ÷¤lµ²¦X«O¯d°Ï¹ï»Ã¯Àµ²ºc¤Î¶Ê¤Æªº¼vÅT¥xÆW­¹«~¬ì§Þ¾Ç·|²Ä39¦¸¦~·|
0981127²Ä¤@§@ªÌ¤j¸z±ìµßk12 ­«²ÕÂùßn°òÐ`??°ò½è¯S²§©Ê¤Î°Ê¤O¾Ç°Ñ¼Æ¤§¬ã¨s¥xÆW­¹«~¬ì§Þ¾Ç·|²Ä39¦¸¦~·|
0961123²Ä¤@§@ªÌ¶ÝÆP©Ê°ª·Åµß bacillus sp. strain TS-23 alpha-¾ý¯»?Ca2+µ²¦X°Ï°ì¤¤223¦ì¸m¤§¾¢®ò»Äªº¬ã¨s»P±´°Q¥xÆW­¹«~¬ì§Þ¾Ç·|²Ä37¦¸
0951124²Ä¤@§@ªÌ¶ÝÆP©Ê°ª·ÅµßBacillus sp. strain TS-23 £\-¾ý¯»?Ói°ò»Ä§Ç¦C¤¤°Ï°ìB¤§¬ã¨s»P±´°Q¥xÆW­¹«~¬ì§Þ¾Ç·|²Ä36¦¸¦~·|
0941125²Ä¤@§@ªÌBacillus sp. TS-23 £\-¾ý¯»¡H¤¤219¦ì¸m¤§¾¢Ói»Ä´Ý°ò¤§¬ðÅܤÀªR¥xÆW­¹«~¬ì§Þ¾Ç·|²Ä35¦¸¦~·|
0931125²Ä¤@§@ªÌStabilization of a Truncated Bacillus sp. Strain TS-23 alpha¡H-Amylase by Replacing Histidine 436 with Aspartate¥xÆW­¹«~¬ì§Þ¾Ç·|²Ä¤T¤Q¥|¦¸¦~·|
* «ü¾É±MÃD©ÎÄvÁÉ
1060309105¾Ç¦~¾Ç¥Í±MÃD¬ã¨s¤Î¹ê°È»s§@ÄvÁÉE. coli prolidase ¤§¥Í¤Æ¯S©Ê¬ã¨s¤ÀªR²Ä¤G¦W
1020314101¾Ç¦~¾Ç¥Í±MÃD¬ã¨s¤Î¹ê°È»s§@ÄvÁÉBacillus licheniformis ¤§NAD(P)+¨Ì¿à«¬îDzæ²B?¿ï¦ì¬ðÅܬã¨s²Ä¤T¦W
1010322¤j¾Ç³¡¦ÛµM¬ì¾ÇÃþ±MÃD¬ã¨s¤fÀY³ø§iACE§í¨îÐ`?¹ï©ó­«²ÕEcDCPªº§í¨î§@¥Î²Ä¤G¦W
100041599¾Ç¦~«×¾Ç¥Í±MÃD¬ã¨sÄvÁÉACE§í¨îÐ`?¹ïE. Coil dipeptidyl carboxypeptidase»Ã¯À¬¡©Êªº¼vÅT¨Î§@
* ±M§Q
* ¾Ç³N©Ê¬ã¨s±M®Ñ¡B±Ð®v±M·~±M®Ñ¡B§Þ³N³ø§i¸ê®Æ