Antarticine-NF3 is a glycoprotein with antifreeze properties produced by the
bacterium Pseudoalteromonas antarctica that has been patented by Spanish
researchers (Parente et al. 2006). It was found that Antarcticine is effective for scar
treatments and re-epithelialization of wounds. This glycoprotein is now included in
some cosmetic regeneration creams (sometimes under the name Antarctilyne). It is
also proposed in association with edelweiss extract: this is of course reminiscent of
the peculiar resistance to harsh conditions of both the Antarctic bacterium and the
Alp flower. The extracts of the Antarctic algae Durvillaea antarctica are included in
cosmetic creams to improve skin vitality such as in the Extra-Firming Day Cream, a
top seller of Clarins (France) (Margesin and Feller 2010). The successful business
endeavor has been the introduction of AFPs into ice cream and yogurt products.
AFPs allow the production of very creamy, dense, reduced fat ice cream with fewer
additives. They control ice crystal growth brought on by thawing on the loading
dock or kitchen table which drastically reduces texture quality (Regand and Goff
2006).
Commercial uses of bacterial INAs for energy and cost saving applications
include the production of artificial snow (Snomax®; the addition of INA to water
in snow-making machines raises the critical temperature for artificial snow making
by several degrees), the production of ice as a construction material for installations
in the Arctic and Antarctica, the manufacture of ice-cream and other frozen food
(Yin et al. 2005), and the substitution for silver iodide in cloud seeding (Lundheim
2002).
6.14.1.3 Molecular Biology Research
Alkaline phosphatases are mainly used in molecular biology for the dephosphorylation of DNA vectors prior to cloning to prevent recircularization, for the dephosphorylation of 5
0 -nucleic acid termini before 5
0 -end labelling by polynucleotide
kinase or for removal of dNTPs and pyrophosphate from PCR. However, the
phosphatase has to be carefully removed after dephosphorylation to avoid
interferences with the subsequent steps. Furthermore, E. coli and calf intestinal
alkaline phosphatase (that was the preferred enzyme for these applications) are
heat-stable and require detergent addition for inactivation. It follows that heatlabile alkaline phosphatases are excellent alternatives as they are inactivated by
moderate heat treatment allowing one to perform the subsequent steps in the same
test tube and minimizing nucleic acid losses. The heat-labile alkaline phosphatase
from Antarctic bacterium is a new tool in molecular biology, this interesting finding
is now well established and expressed in E. coli. This heat-labile alkaline phosphatase sold as Antarctic phosphatase and now proposed to market by New England
Biolabs (USA) (Wang et al. 2007). In the same context, the heat-labile alkaline
phosphatase from the Arctic shrimp Pandalus borealis is also available, for instance,
from Biotec Pharmacon ASA (Norway) or GE Healthcare Life Sciences
(UK) (Margesin and Feller 2010).
6 Plant Growth Promoting Rhizobacteria: Mechanisms and Alleviation of Cold Stress. . . 211
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