本试验旨在探讨固态酶制剂评估中酶的适宜提取液及固-液分离方法。采用4×3双因素完全随机设计，其中提取液分别为去离子水、乙酸-乙酸钠缓冲液（0.1 mol/L，pH 5.50）、磷酸盐缓冲液（0.05 mol/L，pH 6.00）和0.9% NaCl溶液；溶液提取后的固-液分离方法分别为不分离、3 000 r/min离心3 min和中速滤纸过滤。每个处理5个重复，每个重复设2个平行，测定各个处理下酶的活性，并考察提取液的类型对酶制剂产品（α-半乳糖苷酶除外）溶解离心后溶液中溶质及蛋白质含量的影响。结果表明，磷酸盐缓冲液溶解木聚糖酶后活性最高（P<0.05）；乙酸-乙酸钠缓冲液、磷酸盐缓冲液及0.9% NaCl溶液溶解β-葡聚糖酶后活性相当（P>0.05），且均显著地高于去离子水（P<0.05）；去离子水溶解β-甘露聚糖酶后活性最高，其次为乙酸-乙酸钠缓冲液，两者都显著地高于磷酸盐缓冲液和0.9% NaCl溶液（P<0.05）。提取液类型对α-半乳糖苷酶活性无显著影响（P>0.05）。酶制剂溶解后的固-液分离方法对木聚糖酶的测定活性无显著性影响（P>0.05）；提取液离心或过滤后β-葡聚糖酶活性最高（P<0.05）；提取液离心后β-甘露聚糖酶活性最高（P<0.05）；而提取液不分离时α-半乳糖苷酶的活性最高（P<0.05）。提取液的种类和酶制剂溶解后的固-液分离方法对4种非淀粉多糖酶的测定活性有极显著的交互作用（P<0.01）。乙酸-乙酸钠缓冲液对木聚糖酶制剂的溶解度最大（P<0.05），去离子水和0.9% NaCl溶液均对β-葡聚糖酶及β-甘露聚糖酶制剂的溶解度最大（P<0.05）。然而，乙酸-乙酸钠缓冲液溶解木聚糖酶、β-葡聚糖酶、β-甘露聚糖酶后提取液中蛋白质的含量均最低（P<0.05）。上述结果表明，乙酸-乙酸钠缓冲液溶解4种固态酶制剂可以最有效地将酶蛋白提取出来，α-半乳糖苷酶提取后不宜固液分离，而其他3种酶的提取液适宜进行离心分离。

This experiment was conducted to investigate appropriate extract solution and solid-liquid separation method for evaluating enzyme in solid feed enzyme product. Extract solution of deionized water, acetic acid-sodium acetate buffer solution (0.1 mol/L, pH 5.50), phosphate buffer solution (0.05 mol/L, pH 6.00) or 0.9% NaCl solution and solid-liquid separation method of no separation, 3 000 r/min of centrifugation for 3 min or filtration were used in a 4×3 factorial arrangement. Each treatment contained 5 replicates with 2 determination in each. The activities of enzymes in the products were determined. Then, the effects of the types of extract solution on the contents of solute and protein were investigated for the enzyme products (excluding α-galactosidase) dissolved and centrifuged. The results showed that the highest determined activity of xylanase was presented in the phosphate buffer solution buffer solution (P<0.05). The similar determined activities of β-glucanase were observed in acetic acid-sodium acetate buffer solution, phosphate solution and 0.9% NaCl solution (P>0.05), and were significantly higher than that in deionized water (P<0.05). The greatest and greater determined activities of β-mannanase were observed in deionized water and acetic acid-sodium acetate buffer solution, respectively, and were significantly greater than those in phosphate solution or 0.9% NaCl solution (P<0.05). The type of extract solution had no significant effect on the determined activity of α-galactosidase (P>0.05). The solid-liquid separation method had no significant effect on the determined activity of xylanase (P>0.05). The greater determined activity of β-glucanase was observed in centrifugation or filtration (P<0.05). The greatest determined activity of β-mannanase was presented in centrifugation (P<0.05). However, the highest determined activity of α-galactosidase product was observed in no separation (P<0.05). There was a significant interaction between the type of extract solution and solid-liquid separation method in the determined activities of 4 enzyme products (P<0.01). The highest dry matter solubility of xylanase product was observed in acetic acid-sodium acetate buffer solution (P<0.05). The highest dry matter solubility of β-glucanase and β-mannanase was presented in deionized water and 0.9% NaCl solution (P<0.05). However, the lowest protein contents of xylanase, β-glucanase and β-mannanase were observed in acetic acid-sodium acetate buffer solution (P<0.05). It is concluded that acetic acid-sodium acetate buffer solution is the most efficient to extract the enzyme protein from the product. After dissolved, the α-galactosidase product is not suitable to separate, but the other enzymes can be separated with centrifugation.