宋玉琼, 胡晓, 相欢, 陈胜军, 李来好, 杨贤庆, 吴燕燕, 马海霞. 罗非鱼皮胶原肽的酪氨酸酶抑制活性与铜离子结合活性研究[J]. 南方水产科学, 2023, 19(1): 155-164. DOI: 10.12131/20220097
引用本文: 宋玉琼, 胡晓, 相欢, 陈胜军, 李来好, 杨贤庆, 吴燕燕, 马海霞. 罗非鱼皮胶原肽的酪氨酸酶抑制活性与铜离子结合活性研究[J]. 南方水产科学, 2023, 19(1): 155-164. DOI: 10.12131/20220097
SONG Yuqiong, HU Xiao, XIANG Huan, CHEN Shengjun, LI Laihao, YANG Xianqing, WU Yanyan, MA Haixia. Study on tyrosinase inhibitory activity and Cu2+ binding activity of tilapia skin peptides[J]. South China Fisheries Science, 2023, 19(1): 155-164. DOI: 10.12131/20220097
Citation: SONG Yuqiong, HU Xiao, XIANG Huan, CHEN Shengjun, LI Laihao, YANG Xianqing, WU Yanyan, MA Haixia. Study on tyrosinase inhibitory activity and Cu2+ binding activity of tilapia skin peptides[J]. South China Fisheries Science, 2023, 19(1): 155-164. DOI: 10.12131/20220097

罗非鱼皮胶原肽的酪氨酸酶抑制活性与铜离子结合活性研究

Study on tyrosinase inhibitory activity and Cu2+ binding activity of tilapia skin peptides

  • 摘要: 为探明罗非鱼 (Oreochromis) 鱼皮胶原蛋白肽能否有效抑制黑色素的生成,采用酶解法制备出罗非鱼皮酪氨酸酶抑制肽 (Tilapia skin tyrosinase inhibitory peptides, TSTIP),并开展其酪氨酸酶 (Tyrosinase, TYR) 抑制活性与铜离子 (Cu2+) 结合活性的相关性研究。结果显示,罗非鱼皮经碱性蛋白酶酶解4 h后的产物具有最高的TYR抑制活性和Cu2+结合活性,且两者呈极显著正相关 (R=0.856)。荧光光谱分析显示,TSTIP与TYR或Cu2+结合后其内源荧光吸收强度的下降趋势一致,同时紫外吸收增强,且最大吸收波长发生红移。傅里叶变换红外光谱分析显示,TYR与Cu2+主要通过羰基及氨基与TSTIP结合。圆二色谱分析显示,两种结合物中β-转角及无规则卷曲含量相对减少,β-折叠含量相对增多,该现象在TSTIP-Cu2+结合物中更加明显。结果表明,TSTIP结合TYR产生的结构变化与结合Cu2+相似,TSTIP可通过螯合TYR的活性中心Cu2+来抑制其活性。

     

    Abstract: To find out whether the tilapia (Oreochromis) skin collagen peptides can effectively inhibit melanin production, we used enzymatic method to prepare the tilapia skin tyrosinase (TYR) inhibitory peptides (TSTIP) and studied the relevance between TYR inhibitory activity and Cu2+ binding activity. The results show that the product of tilapia skin hydrolyzed by alcalase for 4 h exhibited both the highest TYR inhibitory activity and Cu2+ binding activity, which were significantly positively correlated (R=0.856). When TSTIP was bound to Cu2+ or tyrosinase, the intrinsic fluorescence absorption had a consistent decreasing trend, but the UV absorption increased and the maximum absorption wavelength had a red shift. For FTIR results, TYR and Cu2+ bound to TSTIP mainly by carbonyl and amino groups. Circular dichroism shows that the β-turn and random curl contents of the two conjugates decreased relatively, while the β-fold content increased relatively, which was more obvious for TSTIP-Cu2+ conjugate. In conclusion, the structural change of TSTIP-TYR is similar with that of TSTIP-Cu2+ conjugate, which indicates that TSTIP can inhibit TYR's activity by binding to its Cu2+ active site.

     

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