Anais do Simpósio Latino Americano de Ciências de Alimentos
Anais do 13º Simpósio Latino Americano de Ciência de Alimentos

Coffee roasting is a thermal process that uses temperatures above 200°C and is responsible for the physical, chemical and sensory characteristics that make coffee one of the most appreciated beverages in the world. However, at this stage there is also the formation of acrylamide, a toxic compound and a probable human carcinogen. This substance is formed by Maillard's reaction in foods containing L-asparagine and reducing sugars such as glucose and fructose. L-asparaginase (L-asparagine aminohydrolase EC 3.5.1.1) is an enzyme capable of catalyzing the hydrolysis of L-asparagine to L-aspartic acid and ammonia, thereby reducing the content of L-asparagine, the precursor of this toxic compound. This work aimed to evaluate the potential for acrylamide reduction in coffee by applying L-asparaginases from Aspergillus oryzae IOC 3999 and Aspergillus niger IOC 0203. Samples of 500 g of green arabica coffee beans were steamed for 35 minutes at 100°C to 25% humidity. After heat treatment, the beans were mixed with 345 mL of the purified L-asparaginase solution from Aspergillus oryzae and Aspergillus niger at a concentration of 150 U and incubated for 60 minutes at 60°C and 50°C, respectively. The same procedure was performed with the commercial enzyme Acrylaway® for comparison purposes. After enzymatic treatment, the beans were dried in an oven with air circulation at 40°C to 10.5% humidity and finally roasted at 200°C for 11 minutes to obtain a light roasting degree. The acrylamide content was determined by LC-MS/MS. The reduction in acrylamide content on ground coffee samples was 27.62% using commercial enzyme, 34.92% for A. oryzae L-asparaginase and 18.61% for A. niger L-asparaginase. Enzymes from new fungal strains have great potential for reducing acrylamide in foods.