Nikhita R, Sachindra N M
Department of Meat and Marine Sciences, CSIR- Central Food Technological Research Institute (CFTRI), Mysore, India 570020; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad, India 201002.
Department of Meat and Marine Sciences, CSIR- Central Food Technological Research Institute (CFTRI), Mysore, India 570020; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad, India 201002.
Poult Sci. 2021 May;100(5):101047. doi: 10.1016/j.psj.2021.101047. Epub 2021 Feb 13.
Response surface methodology was adopted to optimize hydrolysis conditions for the production of antioxidant and angiotensin-I converting enzyme (ACE) inhibitory peptides from chicken red blood cells by both enzymatic and acid hydrolysis. During acid hydrolysis, temperature (P < 0.001) and acid concentration (P < 0.001) influenced the degree of hydrolysis (DH%) and 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging activity of the hydrolysate while ACE inhibitory activity of the hydrolysate was strongly influenced by acid concentration (P < 0.001). Temperature and time of hydrolysis had no effect (P > 0.05) on the ACE inhibitory activity of the hydrolysate. Acid hydrolysis conditions of 50°C, 32 h, and 0.03 N hydrochloric acid resulted in optimum DH% (33.1%), optimum DPPH scavenging activity (46%), and optimum ACE inhibitory activity (43.7%) of the hydrolysate. During enzymatic hydrolysis of chicken red blood cells, DH% was influenced by the temperature of hydrolysis (P < 0.001) and enzyme concentration (P < 0.001). DPPH scavenging of the hydrolysate was marginally (P < 0.05) influenced by the temperature of hydrolysis and ACE inhibitory activity of the hydrolysate was highly influenced by temperature (P < 0.001) and enzyme concentration (P < 0.001). Enzyme hydrolysis conditions of 60°C, 150 min, and 2.5% alcalase resulted in maximum DH% of 63.9%, while the highest DPPH scavenging activity (75%) of hydrolysate was observed under the hydrolysis conditions of 60°C, 30 min, and 2.5% of the enzyme. Optimum ACE inhibitory activity (45%) of the hydrolysate was achieved at hydrolysis conditions of 2.5% alcalase, 120 min of hydrolysis at 60°C. ACE inhibitory activity of the enzymatically hydrolyzed product was directly proportional to DH%, while DPPH activity was inversely proportional to DH%. DPPH scavenging activity of the acid hydrolysate was recorded at a lower range (34.8-56.9%) compared to the enzyme hydrolysate (40.4-77.4%), while ACE inhibitory activity of both the hydrolysates was observed in the same range (18.7-49.4 and 14.2-47.7% for acid and enzyme hydrolysate, respectively). This study indicated that chicken red blood cells could be successfully hydrolyzed by both chemical and enzymatic methods to obtain hydrolysates having antioxidant and ACE inhibitory activity.
采用响应面法优化酶解和酸解从鸡红细胞中生产抗氧化剂和血管紧张素I转换酶（ACE）抑制肽的水解条件。在酸解过程中，温度（P<0.001）和酸浓度（P<0.001）影响水解度（DH%）和水解产物的1,1-二苯基-2-苦基肼（DPPH）自由基清除活性，而水解产物的ACE抑制活性受酸浓度的强烈影响（P<0.001）。水解温度和时间对水解产物的ACE抑制活性没有影响（P>0.05）。50°C、32小时和0.03N盐酸的酸解条件导致水解产物的最佳水解度（33.1%）、最佳DPPH清除活性（46%）和最佳ACE抑制活性（43.7%）。在鸡红细胞的酶解过程中，水解度受水解温度（P<0.001）和酶浓度（P<0.001）的影响。水解产物的DPPH清除率受水解温度的轻微影响（P<0.05），而水解产物的ACE抑制活性受温度（P<0.001）和酶浓度（P<0.001）的高度影响。60°C、150分钟和2.5%碱性蛋白酶的酶解条件导致最大水解度为63.9%，而在60°C、30分钟和2.5%酶的水解条件下观察到水解产物的最高DPPH清除活性（75%）。在2.5%碱性蛋白酶、60°C水解120分钟的水解条件下，水解产物达到最佳ACE抑制活性（45%）。酶解产物的ACE抑制活性与水解度成正比，而DPPH活性与水解度成反比。与酶解产物（40.4-77.4%）相比，酸解产物的DPPH清除活性记录在较低范围（34.8-56.9%），而两种水解产物的ACE抑制活性在相同范围内观察到（酸解产物和酶解产物分别为18.7-49.4%和14.2-47.7%）。本研究表明，鸡红细胞可以通过化学和酶法成功水解，以获得具有抗氧化和ACE抑制活性的水解产物。
