Journal
FOOD CHEMISTRY
Volume 141, Issue 3, Pages 2974-2981Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2013.05.132
Keywords
Achaetomium sp Xz8; Endo-polygalacturonase; Low-temperature-active; High specific activity; Juice clarification
Funding
- National Natural Science Foundation of China [31271937]
- National High Technology Research and Development Program of China [2012AA022207A]
- China Modern Agriculture Research System [CARS-42]
- 948 program of the Ministry of Agriculture [2011-G7-4]
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A novel endo-polygalacturonase (endo-PG I) from Achaetomium sp. Xz8 was identified, overexpressed in Pichia pastoris, and characterized in this report. Recombinant endo-PG I is distinguished from other enzyme counterparts by its high activity towards polygalacturonic acid (49,934 U/ml) and high yield in the 15-1 fermentor (2.13 g/l). It exhibits optimal activity at 45 C and remained active over a broad temperature range of 0-80 degrees C. Distinct from most fungal polygalacturonases that have acidic pH optima, endo-PG I is optimally active at pH 6, similar to the pH of fresh papaya juice (5.7). Endo-PG I alone reduced the viscosity of papaya juice by 17.6%, and increased its transmittance by 59.1%. When combined with a commercial pectin methylesterase, it showed much higher efficiency with a synergy degree of more than 1.25. All these favourable enzymatic properties make endo-PG I attractive for potential applications in the juice industry. (C) 2013 Elsevier Ltd. All rights reserved.
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