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L-asparaginase Production by a new isolate Bacillus aryabhattai strain ITBHU02 in solid state culture

ABSTRACT The enzyme, L-asparaginase (L-asparagine amino hydrolase, EC 3.5.1.1), catalyzes L-
asparagine breakdown into aspartic acid and ammonia. In recent years, asparaginases have been
receiving meticulous attention because of their potential medicinal uses and application in food
industries. This study presents production of L-asparaginase by a new isolate Bacillus
aryabhattai Strain ITBHU02 on the solid surface of rice husk, wheat bran, rice bran, cotton seed
powder, coconut oil cake, and groundnut oil cake as substrates. Optimization of the solid state
fermentation media and parameters resulted in a 14% increase in the L-asparaginase activity.
Optimum L-asparaginase production 16.1 U/gds was observed on wheat bran supplemented with
1%, (w/w) yeast extract, 0.25%, (w/w) L-asparagine at pH 7.5, 100%, (v/w) initial moisture and
30°C after incubation 36 hrs.

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    ABSTRACT: Acrylamide formation in French fries was investigated in relation to blanching and asparaginase soaking treatments before final frying. Par-fried potatoes of Bintje variety were prepared by cutting strips (0.8 × 0.8 × 5 cm) which were blanched at 75 °C for 10 min. Unblanched strips were used as the control. Control or blanched strips were then dried at 85 °C for 10 min and immediately partially fried at 175 °C for 1 min. Finally, frozen par-fried potatoes were fried at 175 °C for 3 min to obtain French fries. Pre-drying of raw or blanched potato strips did not generate acrylamide formation as expected. Partial frying of pre-dried control potato strips generated 370 μg/kg of acrylamide and the final frying determined French fries with 2075 μg/kg of acrylamide. When control potato strips were treated with a 10000 ASNU/l asparaginase solution at 40 °C for 20 min, the acrylamide formation in French fries was reduced by 30%. When blanched potato strips were treated in the same way, the produced French fries have 60% less acrylamide content than blanched strips without the enzyme treatment. Soaking of blanched potato strips (75 °C, 10 min) in an 10000 ASNU/l asparaginase solution at 40 °C for 20 min is an effective way to reduce acrylamide formation after frying by reducing the amount of one of its important precursors such as asparagine.
    Food Chemistry. 01/2008;
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    ABSTRACT: This article comprises detailed information about L-asparaginase, encompassing topics such as microbial and plant sources of L-asparaginase, treatment with L-asparaginase, mechanism of action of L-asparaginase, production, purification, properties, expression and characteristics of l-asparaginase along with information about studies on the structure of L-asparaginase. Although L-asparaginase has been reviewed by Savitri and Azmi (2003), our effort has been to include recent and updated information about the enzyme covering new aspects such as structural modification and immobilization of L-asparaginase, recombinant L-asparaginase, resistance to L-asparaginase, methods of assay of L-asparagine and L-asparaginase activity using the biosensor approach, L-asparaginase activity in soil and the factors affecting it. Also, side-effects of L-asparaginase treatment in acute lymphoblastic leukemia (ALL) have been discussed in the current review. L-asparaginase has been and is still one of the most widely studied therapeutic enzymes by researchers and scientists worldwide.
    Critical Reviews in Biotechnology 01/2007; 27(1):45-62. · 5.10 Impact Factor
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    ABSTRACT: Production of a tumor-inhibitory asparaginase by submerged fermentation with Serratia marcescens ATCC 60 was studied to ascertain optimal nutritional conditions for large-scale production leading to enzyme purification studies. Five strains of S. marcescens were screened in shake-flask studies and were found to produce 0.8 to 3.7 IU/ml 48 hr after inoculation. The requirements for asparaginase production with S. marcescens ATCC 60, the high producing strain, included the following: 4% autolyzed yeast extract medium (initial pH 5.0), an incubation temperature of 26 C, and limited aeration for a zero level of dissolved oxygen during the fermentation. Addition of various carbohydrates to the fermentation medium did not enhance yields. The peak cell population in the fermentation medium and the maximal asparaginase yields occurred simultaneously. Highest enzyme yields were found when the pH of the fermentation cycle rose to approximately 8.5. Yields of 4 IU of asparaginase/ml of cell suspension have been obtained consistently in 40 to 42 hr from 10-liter volumes (500 ml/4-liter bottle) produced on a reciprocating shaker. Scale-up to a 60-liter fermentor yielded 3.1 IU/ml in 35 hr.
    Applied microbiology 11/1969; 18(4):550-4.

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May 31, 2014