@article { ISI:000311754600007,
	title = {Antibacterial properties of linolenic sophorolipid and its chemically esterified methyl ester form},
	journal = {Research Journal of Biotechnology},
	volume = {7},
	number = {3},
	year = {2012},
	month = {AUG},
	pages = {40-45},
	publisher = {RESEARCH JOURNAL BIOTECHNOLOGY},
	address = {SECTOR A-80, SCHEME NO 54, VIJAY NAGAR, A B ROAD, INDORE, 452 010 MP, INDIA},
	abstract = {<p>The antibacterial activity of Linolenic SL mixture (containing 80\% lactone) and its methyl ester derivative against Gram positive (B. subtilis) and Gram negative (E. coli and P. aeruginosa) bacteria is reported here. Bacterial cultures were treated with increasing concentrations of Linolenic SL mixture and its methyl ester derivative and antibacterial activity was checked at different time-intervals (2, 4 and 6 hrs) using standard dilution micromethod and spread plate method. Decrease in bacterial colonies was observed with increase in concentrations of compounds as well as incubation time but the level of effectiveness varies with the compound and bacteria. The minimum inhibitory concentrations (MIC) of Linolenic SL mixture (LNNSL, containing 80\% lactone) against B. subtilis, E. coli and P. aeruginosa were found to be 20, 10 and 10 mu g ml(-1) respectively. The MIC values of methyl ester form (LNNSLME) against B. subtilis, E. coli and P. aeruginosa were determined to be \&gt;20, 20 and 20 mu g ml(-1) respectively. The results suggest that Linolenic SL mixture (containing 80\% lactone) as compared to its methyl ester derivative showed good antibacterial activity towards both the Gram positive and Gram negative bacteria and were found to be more potent against Gram negative bacteria.</p>},
	keywords = {antibacterial activity, Bacillus subtilis, Escherichia coli, Linolenic sophorolipid mixture, Minimum inhibitory concentration, Pseudomonas aeruginosa, Sophorolipid methyl ester},
	issn = {0973-6263},
	author = {Reetika, Gupta and Kumar, Uma S. and Asmita, Prabhune}
}
@article { ISI:000300202400005,
	title = {Purification and characterization of YxeI, a penicillin acylase from Bacillus subtilis},
	journal = {International Journal of Biological Macromolecules},
	volume = {50},
	number = {1},
	year = {2012},
	month = {JAN},
	pages = {25-30},
	publisher = {ELSEVIER SCIENCE BV},
	address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS},
	abstract = {<p>The paper reports the purification and characterization of the first penicillin acylase from Bacillus subtilis. YxeI, the protein annotated as hypothetical, coded by the gene yxeI in the open reading frame between iol and hut operons in B. subtilis was cloned and expressed in Eshcherichia coli, purified and characterized. The purified protein showed measurable penicillin acylase activity with penicillin V. The enzyme was a homotetramer of 148 kDa. The apparent Km of the enzyme for penicillin V and the synthetic substrate 2-nitro-5-(phenoxyacetamido)-benzoic acid was 40 mM and 0.63 mM, respectively, and the association constants were 8.93 x 10(2) M-1 and 2.51 x 10(5) M-1, respectively. It was inhibited by cephalosporins and conjugated bile salts, substrates of the closely related bile acid hydrolases. It had good sequence homology with other penicillin V acylases and conjugated bile acid hydrolases, members of the Ntn hydrolase family. The N-terminal nucleophile was a cysteine which is revealed by a simple removal of N-formyl-methionine. The activity of the protein was affected by high temperature, acidic pH and the presence of the denaturant guanidine hydrochloride. (C) 2011 Elsevier B.V. All rights reserved.</p>},
	keywords = {Bacillus subtilis, Conjugated bile acid hydrolases, Ntn hydrolase, Penicillin acylase},
	issn = {0141-8130},
	doi = {10.1016/j.ijbiomac.2011.09.018},
	author = {Rathinaswamy, Priya and Gaikwad, Sushama M. and Suresh, C. G. and Prabhune, Asmita and Brannigan, James A. and Dodson, Guy G. and Pundle, Archana V.}
}
