RT Journal Article SR Electronic(1) A1 Von Tigerstrom, R. G. A1 Stelmaschuk, S.YR 1987 T1 Purification and Partial Characterization of an Amylase from Lysobacter brunescens JF Microbiology, VO 133 IS 12 SP 3437 OP 3443 DO https://doi.org/10.1099/00221287-133-12-3437 PB Microbiology Society, SN 1465-2080, AB SUMMARY: Four species of the genus Lysobacter, especially L. brunescens and L. gummosus, produced amylase when grown in liquid medium containing starch. The amylase was purified nearly 1200-fold with a 36% yield from the culture supernatant of L. brunescens by ammonium sulphate precipitation, CM-52 cellulose chromatography and gel filtration. An M r of 47000–49000 was estimated for the enzyme from results of SDS-PAGE and glycerol gradient centrifugation, respectively. Metal ions such as Mg2+, Ca2+, Mn2+ or Zn2+ are not required for activity. The amylase is active from pH 5.0 to 7.5, degrades starch endohydrolytically and has a K m of 2.08 mg starch ml-1. Amylopectin, amylose and glycogen were also hydrolysed. Dextran, maltose, maltotriose, maltotetraose and 4-nitrophenyl α-d-glucoside were hydrolysed very slowly, or not at all. Other enzymes capable of degrading starch, maltose or malto-oligosaccharides were not detected in the culture supernatant of L. brunescens. , UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-133-12-3437