February 15-18, 2009 Washington State Convention Center Seattle ...

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CULTURE OF Gracilaria corticata IN THE EARTHEN PONDS OF BERIS SESSION
(CHABAHAR)
Abdollah Haghpanah, Lalik Sarikhani, Yousof Irii and Behrooz Gharavy
Fishery Research Center of Golestan
The study of Gracilaria cultuer was carried out from October 2000 to Sebtember 2001 during 4 seasons in the earthen ponds
. Water depth in ponds was 110 Cm. Culture system was fixed bottom line method. In this study 500 gram gracilaria were
cultured on the line and investigated about 9 weeks. Gracilaria reached to maximum growth in 6 to 7 weeks and biomas were
2.3 time in the atumn, 2.6 time in winter, 2,7 in spring and 2.4 in summer respectivaly. One way Anova showed that average
weight was not similar in various season and showed significant difference. The avearage daily growth rate in different season
was between 4.3 to 34.3 grams too.
CLONING, EXPRESSION AND PURIFICATION OF BETA-AGARASE II FROM
Saccharophagus sp. AG21
Youngdeuk Lee, Kwangsun Jung, Jihee Lim, Se Jae Kim and Jehee Lee
Department of Marine Biotechnology
College of Ocean Science
Cheju National University
Jeju, 690-756, Republic of Korea
Agar is an important gelifying agent for biochemical use and the food industry. Agar is a polysaccharide which linked
D-galactose and L-3,6-anhydro-galactose residues. Beta-agarase cleave 1,4-β-linkage. The named beta-agarase β -agarases are
classified into two groups named as β -agarase I and II based on their cleavage of β-(1→4) linkages. Main hydrolyzed products
of β-agarase I are neoagarotetrose and neoagarohexaose, while β -agarase II produces the neoagarobiose.
We screened agarase producing marine bacteria from seawater of Jeju island. We isolated genomic DNA from the bacteria
and analyzed 16s rRNA sequence by PCR and sequencing. The sequence was 99% (1376/1384 bp) similar to Saccharophagus
degradans 2-40. We determine the ORF sequence of agarase (agaY2). We Clone, over expression and purification of
recombinant protein using E. coli expression system. We analyze reaction products of recombinant protein by thin layer
chromatography.
The 2334 base pair ORF of agaY2 agarase is encoding 778 amino acid residues. The predicted agaY2 has molecular mass of
88 kDa and and isoelectric porint 5.2. Pair wise amino acid comparison of agarase showed 96% highes level of identity with
Saccharophagus degradans 2-40 agarase. The purified recombinant agaY2 was not able to degrade agar, however it could
only degrade the neoagarotetraose and neoagarohexaose, mainly into neoagarobiose components. AgaY2 showed functional
character of beta-agarse II.