肌浆蛋白对来自金线鱼属（Nemipterus spp.）的丝氨酸蛋白酶抑制剂的活性。

Proteinase inhibitory activity of sarcoplasmic proteins from threadfin bream (Nemipterus spp.).

机构信息

School of Food Technology, Institute of Agricultural Technology, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand.

出版信息

J Sci Food Agric. 2010 Jan 30;90(2):291-8. doi: 10.1002/jsfa.3814.

DOI:10.1002/jsfa.3814

PMID:20355045

Abstract

BACKGROUND

Thailand is the second largest surimi producer in the world and 50% of surimi is produced from threadfin bream. During surimi processing, sarcoplasmic proteins are removed through water washing and discarded in the waste stream. This study was aimed at investigating the proteinase inhibitory activity of sarcoplasmic proteins.

RESULTS

Sarcoplasmic proteins from threadfin bream (TBSP) exhibited inhibitory activity toward trypsin but did not inhibit papain and chymotrypsin. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis under non-reducing condition stained by trypsin inhibitory activity revealed three protein bands of molecular mass of 95, 41 and 37 kDa. Inhibitory activity of TBSP reached a maximum when subjected to 45 degrees C and completely disappeared at 60 degrees C. The breaking force and deformation of lizardfish surimi gel with added TBSP and pre-incubated at 37 degrees for 20 min increased with additional levels of TBSP (P < 0.05). Trichloroacetic acid-oligopeptide content of lizardfish surimi gel with added TBSP decreased with the addition of 4 g kg(-1) TBSP (P < 0.05). Retention of myosin heavy chain (MHC) increased when TBSP concentration was increased. TBSP effectively protected MHC from proteolysis at 37 degrees C to a similar extent as egg white powder, but efficacy of TBSP was not observed at 65 degrees C.

CONCLUSION

TBSP could be applied to reduce proteolytic degradation of lizardfish surimi or other surimi associated with trypsin-like proteinase, rendering an improvement in surimi gelation set at 37-40 degrees C.

摘要

背景

泰国是世界上第二大鱼糜生产国，其中 50%的鱼糜由金线鱼制成。在鱼糜加工过程中，肌浆蛋白通过水洗去除，并在废水流中丢弃。本研究旨在研究肌浆蛋白的蛋白酶抑制活性。

结果

金线鱼肌浆蛋白（TBSP）对胰蛋白酶具有抑制活性，但对木瓜蛋白酶和胰凝乳蛋白酶没有抑制作用。非还原条件下经胰蛋白酶抑制活性染色的十二烷基硫酸钠-聚丙烯酰胺凝胶电泳显示，分子量为 95、41 和 37 kDa 的 3 条蛋白质带。TBSP 的抑制活性在 45°C 时达到最大值，在 60°C 时完全消失。添加 TBSP 并在 37°C 下预孵育 20 分钟的蜥蜴鱼鱼糜凝胶的断裂力和变形随着 TBSP 添加量的增加而增加（P < 0.05）。添加 TBSP 的蜥蜴鱼鱼糜凝胶中的三氯乙酸-寡肽含量随着 4 g/kg TBSP 的添加而降低（P < 0.05）。随着 TBSP 浓度的增加，肌球蛋白重链（MHC）的保留增加。TBSP 可有效保护 MHC 在 37°C 下免受蛋白水解，其效果与蛋清粉相当，但在 65°C 下未观察到 TBSP 的效果。