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Secretion of Mouse α-Amylase fromKluyveromyces lactis

✍ Scribed by TOKUNAGA, MASAO; ISHIBASHI, MATSUJIRO; TATSUDA, DAISUKE; TOKUNAGA, HIROKO

Publisher: John Wiley and Sons
Year: 1997
Tongue: English
Weight: 127 KB
Volume: 13
Category: Article
ISSN: 0749-503X
DOI: 10.1002/(sici)1097-0061(19970630)13:8<699::aid-yea124>3.0.co;2-n

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✦ Synopsis

We constructed two mouse -amylase secretion vectors for Kluyveromyces lactis using the well-characterized signal sequence of the pGKL 128 kDa killer precursor protein. Both PHO5 and PGK expression cassettes from Saccharomyces cerevisiae directed the expression of mouse -amylase in YPD medium at a similar level of efficiency. K. lactis transformants secreted glycosylated and non-glycosylated -amylase into the culture medium and both species were enzymatically active. The K. lactis/S. cerevisiae shuttle secretion vector pMI6 was constructed, and K. lactis MD2/1(pMI6) secreted about four-fold more -amylase than S. cerevisiae YNN27 harboring the same plasmid, indicating that K. lactis is an efficient host cell for the secretion and production of recombinant proteins.

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