Protein profiles and DNA isolation of hemolymph gonggong snail (Strombus sp.) from Bintan

3rd EMBRIO International Workshop on Marine Biodiversity: Understanding, Utilization, Conservation

生态环境科学

Viruly, L.^1 ; Andarwulan, N.^2 ; Suhartono, M.T.^2 ; Nurilmala, M.^3

Department of Aquatic Product Technology, Raja Ali Haji Maritime University, Tanjungpinang, Riau Islands, Indonesia^1

Department of Food Science and Technology, Bogor Agricultural University, Bogor, Indonesia^2

Department of Aquatic Product Technology, Bogor Agricultural University, Bogor, Indonesia^3

关键词: Antimicrobial peptide;    Bintan;    Bioactive peptides;    DNA isolation;    Histone proteins;    Protein profiles;    Protein profiling;    snail;   

Others  :  https://iopscience.iop.org/article/10.1088/1755-1315/278/1/012078/pdf
DOI  :  10.1088/1755-1315/278/1/012078

学科分类：环境科学（综合）

来源: IOP

【 摘 要 】

Gonggong snail is one of the famous and highly-priced local seafood in Bintan Island, Riau Islands Province. It is an icon of Tanjung Pinang city. Until now, general research on Bintan gonggong snail is scarce, even if it has the potential to be used for aquaculture, functional food ingredient, and medicine. Research of bioactive peptides are mostly performed using the group of molluscs (gastropods). The research on protein profiles and DNA isolation has never been studied in hemolymph Bintan gonggong snail. This research was aimed to identify protein profiles and DNA isolation in hemolymph Bintan gonggong snail (Strombus sp). Protein profiling used SDS-PAGE. DNA isolation used Qiagen DNeasy methods, while PCR used primer histon H2A. Identification on protein profiles displayed that thin-shelled and thick-shelled gonggong snails had a similiarity value of 37 kDa, whereas the other protein profiles were different. The types of protein of Bintan gonggong snails were predicted to be histone proteins. The DNA of hemolymph Bintan gonggong snails had a similiarity value of 75 bp fragment histon. It is predicted as protein histon H2A and will be developed potentially as antimicrobial peptides (AMPs).