(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Terrabacteria group: NE > Actinobacteria [phylum]: NE > Actinobacteria [class]: NE > Micrococcales: NE > Intrasporangiaceae: NE > Janibacter: NE > Janibacter sp. HTCC2649: NE
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MELSMPLRLTRVMPALVAAAAAVALLPQSASAATVAADPVGPEQISFLPA KLYSSLAPTALPPGTNDWTCQPSAAHPRPVVLVHGTWANRYDSFAMIAPH LKRAGYCVYALNYGDENVSVLGQLPGLYATQTIKPAGGEISSFVDQVLDS TGADQVDMFGWSQGGIAARSYLKFYGGTNAANPAANKVKNLITFGATNHG TTLSGLGALAGQLAPATIPPVLGPAAADQLIDSPFLTELNAGGDTQPGVT YTIIGSRYDEVSTPYQRTFLTAGPGATVNNITLQNGCEIDLSDHLSGLYS YRLVGLVKKALDPTGNVYVPCLPNAPVL
References
Title: A novel sn-1,3 specific lipase from Janibacter sp. as catalysts for the high-yield synthesis of long-medium-long type structured triacylglycerols Cui R, Xu L, Lan D, Yang B, Wang Y Ref: Food Chem, 366:130523, 2021 : PubMed
Our study offers a novel sn-1,3 specific lipase MAJ1 from marine member Janibacter sp. strain HTCC2649 for preparing long-medium-long (LML) type structured triacylglycerols (TAGs). Firstly, the resin ECR1030 was selected as a suitable support for the immobilization of lipase MAJ1. An efficient synthesis of LML-type structured TAGs by the immobilized lipase MAJ1-catalyzed interesterification of methyl palmitate and tricaprylin was studied in a solvent-free system. The reaction conditions, including substrate molar ratio, temperature and enzyme loading, were optimized. Under the optimum conditions (immobilized lipase MAJ1 of 45 U/g, substrate molar ratio of 4:1, temperature of 35 degreesC, reaction time of 24 h), the structured TAGs with double long chains (DLCST) were obtained in a yield of 44.3 mol%. Secondly, multi-dimensional mass spectrometry-based shotgun lipidomics (MDMS-SL) was employed to quantify each TAG positional isomer in DLCST. The content of 1,3-dipalmitoyl-2-capryloyl-sn-glycerol in DLCST was 97.6% determined by the MDMS-SL technology.
Title: Biochemical properties of a new cold-active mono- and diacylglycerol lipase from marine member Janibacter sp. strain HTCC2649 Yuan D, Lan D, Xin R, Yang B, Wang Y Ref: Int J Mol Sci, 15:10554, 2014 : PubMed
Mono- and di-acylglycerol lipase has been applied to industrial usage in oil modification for its special substrate selectivity. Until now, the reported mono- and di-acylglycerol lipases from microorganism are limited, and there is no report on the mono- and di-acylglycerol lipase from bacteria. A predicted lipase (named MAJ1) from marine Janibacter sp. strain HTCC2649 was purified and biochemical characterized. MAJ1 was clustered in the family I.7 of esterase/lipase. The optimum activity of the purified MAJ1 occurred at pH 7.0 and 30 degrees C. The enzyme retained 50% of the optimum activity at 5 degrees C, indicating that MAJ1 is a cold-active lipase. The enzyme activity was stable in the presence of various metal ions, and inhibited in EDTA. MAJ1 was resistant to detergents. MAJ1 preferentially hydrolyzed mono- and di-acylglycerols, but did not show activity to triacylglycerols of camellia oil substrates. Further, MAJ1 is low homologous to that of the reported fungal diacylglycerol lipases, including Malassezia globosa lipase 1 (SMG1), Penicillium camembertii lipase U-150 (PCL), and Aspergillus oryzae lipase (AOL). Thus, we identified a novel cold-active bacterial lipase with a sn-1/3 preference towards mono- and di-acylglycerides for the first time. Moreover, it has the potential, in oil modification, for special substrate selectivity.
Janibacter sp. strain HTCC2649 is a novel marine member of the Actinobacteria, family Intrasporangiaceae, and is closely related to Janibacter melonis CM2104(T) and Knoellia sinensis HKI 0119(T). The organism was isolated from a sample collected at Hydrostation S south of Bermuda by using high-throughput culturing techniques. Here we present the genome sequence of Janibacter sp. strain HTCC2649.
