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Glucose oxidase (GOx) with high enzyme activity at low temperature (4°C) is potentially useful for food preservation, especially for aquatic products preservation. A cold-active GOx with approximately 83% similarity to known protein sequences, was isolated from  Penicillium  sp. MX3343 and expressed in  Pichia pastoris  X33. Through high cell density fermentation, the yield of recombinant enzyme (named GOxP 5 ) reached 458.6 U/mL. GOxP 5  showed optimal activity at 30°C and pH 5.5, and was stable at a broad pH range from pH 2–6. Moreover, GOxP 5  could maintain 72% maximum activity at 4°C, suggesting its application for the preservation of aquatic products at low-temperatures. Importantly, GOxP 5  showed a good antimicrobial effect against common fish pathogenic bacteria ( Listeria monocytogenes  and  Vibrio parahaemolyticus ). Moreover, sensory, microbiological (total bacterial count), and physicochemical (total volatile basic nitrogen and pH) systematic analyses proved GOxP 5  to be an excellent freshness preserving agent in the context of the grass carp. These favorable enzymatic properties of GOxP 5  make it potentially useful in food biopreservation, and the effect was better compared to the commonly used chemical preservatives.

A New Cold-Active Glucose Oxidase From Penicillium: High-Level Expression and Application in Fish Preservation