Investigation of lactams
The recen t ly developed methods of synthesizing substi tuted 1H,2,3 ,4te t rahydroazepino[3,4-b] indoles [1-3] f rom cap ro l ac t am have opened broad pe r spec t ives for p repar ing condensed lndole de r iva t ives of biological in te res t [4]. In pa r t i cu la r , it became of in te res t to synthesize the indole analogs of such biological ly active compounds as Corazol ( a f t p e n t a m e t h y l e n e t e t r a z o l e ) [5], Omethy lcapro lac t im [6], and also a s e r i e s of 1,2and 10-subst i tu ted azepino[3,4b]indoles for pharmacologica l investigation.
Säureamid‐Reaktionen, XLIII. Über Säureamid‐Dimethylsulfat‐Addukte
Die Dimethylsulfat-Addukte von N.N-Dialkyl- saureamiden, N-alkyl-substituierten cyclischen Amiden sowie von Bis-dialkylamiden einiger Dicarbonsauren werden beschrieben.
Effect of Aeration and Agitation Regimes on Lipase Production by Newly Isolated Rhodotorula mucilaginosa–MTCC 8737 in Stirred Tank Reactor Using Molasses as Sole Production Medium
The influence of media and process parameters (aeration and agitation) on fermentation broth rheology and biomass formation has been studied in 1.5-l stirred tank reactor for lipase production using Rhodotorula mucilaginosa MTCC 8737. Molasses, as sole production medium, is used for lipase production by varying aeration (1, 2, and 3 vvm) and agitation speeds (100, 200, and 300 rpm). Maximum lipase activity of 72 U/ml was obtained during 96 h of fermentation at 2 vvm, 200 rpm, pH 7, and 25 ± 2°C temperature. Lipase production kinetics with respect to dry cell weight of biomass showed YP/S of 25.71 U/mg, specific product formation of 10.9 U/mg DC, and YX/S 2.35 mg/mg. Maximum lipase activity (MC 2) of 56 U/ml was observed at 1% molasses, and a further increase in the molasses concentration of (%) 1.5 and 2 inhibited the product formation of lipase with 15 and 8.5 U/ml, respectively. The production kinetics of molasses media showed YP/X was 14 U/mg DC, YP/S 16 U/mg, and YX/S 1.14 mg/mg during 96 h of bioreactor operation. The kLa values for all batches (MC 1–MC 4) at 96 h of fermentation were 32, 28, 21, and 19/h, and the |oxygen transfer rate were 54.4, 56, 35.7, and 17.29 mg/l h, respectively. Increase in molasses concentration resulted in decreased lipase activity by increase in viscosity of the fermentation broth.