The xylanase (xysA) and the cellulase (celA1) genes from Streptomyces halstedii JM8 were cloned into Escherichia coli/Brevibacterium lactofermentum shuttle vectors and successfully expressed in both hosts when placed downstream from the kanamycin resistance promoter (Pkan) from Tn5 but not when under the control of their own promoters. Xylanase was secreted into the culture media of B. lactofermentum by removal of the same leader peptide as is removed in S. halstedii. The main difference between the production of xylanase by Streptomyces and corynebacteria was the low level of processing of the mature extracellular xylanase by B. lactofermentum, probably due to the lack of protease activity in this microorganism.
|الصفحات (من إلى)||91-97|
|دورية||Archives of Microbiology|
|المعرِّفات الرقمية للأشياء|
|حالة النشر||Published - ديسمبر 2001|
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