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Candida antarctica lipase B (CalB) was efficiently expressed (6.2 g L–1) in Escherichia coli by utilizing an N-terminal tag cassette and the XylS/Pm expression system in a fed-batch bioreactor; subsequent direct binding to EziG from crude extracts resulted in an immobilized catalyst with superior activity to Novozym 435.
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Cassimjee et al. (2017) studied this question.
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