首页> 美国卫生研究院文献>Marine Drugs >Thermal Transition Properties of Hoki (Macruronus novaezelandiae) and Ling (Genypterus blacodes) Skin Collagens: Implications for Processing
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Thermal Transition Properties of Hoki (Macruronus novaezelandiae) and Ling (Genypterus blacodes) Skin Collagens: Implications for Processing

机译:Hoki(Macruronus novaezelandiae)和Ling(Genypterus blacodes)皮肤胶原蛋白的热转变特性:对加工的意义

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摘要

Hoki (Macruronus novaezelandiae) and ling (Genypterus blacodes) are cold-water fish caught in New Zealand waters. Their skins are a major component of the post-processing waste stream. Valuable products could be developed from the skins, as they are primarily composed of collagen, which has many commercial applications. We prepared acid soluble collagens (ASC) from hoki and ling skins, and analyzed their thermal denaturation properties using a Rapid Visco™ Analyzer. At slower heating rates the denaturation temperature (TD) of hoki and ling collagens decreased. This result is consistent with the model of irreversible rate kinetics for the denaturation of collagen. We determined the effects of solvents that disrupt hydrogen bonding on ASC stability. Increasing concentrations of urea from 0.1 M to 1.0 M and acetic acid from 0.1 M to 0.5 M decreased TD. This resulted from the effects of these reagents on the hydrogen bonds that stabilize the collagen triple helix.
机译:Hoki(Macruronus novaezelandiae)和ling(Genypterus blacodes)是在新西兰水域捕获的冷水鱼。它们的皮肤是后处理废物流的主要组成部分。可以从皮肤开发有价值的产品,因为它们主要由胶原蛋白组成,具有许多商业应用。我们从hoki和ling皮肤中制备了酸溶性胶原蛋白(ASC),并使用Rapid Visco™分析仪分析了它们的热变性特性。在较低的加热速率下,hoki和ling胶原的变性温度(TD)降低。该结果与胶原变性的不可逆速率动力学模型一致。我们确定了破坏氢键的溶剂对ASC稳定性的影响。尿素浓度从0.1 M增加到1.0 M,乙酸浓度从0.1 M增加到0.5 M会降低TD。这是由于这些试剂对稳定胶原三螺旋的氢键的影响所致。

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