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聚(L-丙交酯)/无规聚(3-羟基丁酸酯)共混物的相结构与酶降解:原子力显微镜研究

Phase structure and enzymatic degradation of poly(L-lactide)/atactic poly(3-hydroxybutyrate) blends: an atomic force microscopy study.

作者信息

Kikkawa Yoshihiro, Suzuki Takayuki, Tsuge Takeharu, Kanesato Masatoshi, Doi Yoshiharu, Abe Hideki

机构信息

Nanoarchitectonics Research Center, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba Central 4, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8562, Japan.

出版信息

Biomacromolecules. 2006 Jun;7(6):1921-8. doi: 10.1021/bm0600163.

Abstract

Phase structures and enzymatic degradation of poly(l-lactide) (PLLA)/atactic poly(3-hydroxybutyrate) (ata-PHB) blends with different compositions were characterized by using atomic force microscopy (AFM). Differential scanning calorimetry (DSC) thermograms of PLLA/ata-PHB blends with different compositions showed two glass transition temperatures, indicating that the PLLA/ata-PHB blends are immiscible in the melt. Surface morphologies of the thin films for PLLA/ata-PHB blends were determined by AFM. Phase separated morphology was recognized from the AFM topography and phase images. The domain size of the components was dependent on the blend ratio. Enzymatic degradation of the PLLA/ata-PHB blends was performed by using both PHB depolymerase and proteinase K. Either PLLA or ata-PHB domains were eroded depending on the kinds of enzyme. Surface morphologies after enzymatic degradation have revealed the phase structure along the depth direction. Enzymatic adsorption of PHB depolymerase was examined on the surface of PLLA/ata-PHB blends. The enzyme molecules were found on both domains of the binary blends. The larger number of enzyme molecules was found on the PLLA domains relative to those on the ata-PHB domains, suggesting the higher affinity of the enzyme against PLLA domain.

摘要

采用原子力显微镜(AFM)对不同组成的聚(L-丙交酯)(PLLA)/无规聚(3-羟基丁酸酯)(无规-PHB)共混物的相结构和酶促降解进行了表征。不同组成的PLLA/无规-PHB共混物的差示扫描量热法(DSC)热谱图显示出两个玻璃化转变温度,这表明PLLA/无规-PHB共混物在熔体中是不相容的。通过AFM测定了PLLA/无规-PHB共混物薄膜的表面形貌。从AFM形貌和相图像中识别出相分离形态。组分的畴尺寸取决于共混比。使用PHB解聚酶和蛋白酶K对PLLA/无规-PHB共混物进行酶促降解。根据酶的种类,PLLA或无规-PHB畴会被侵蚀。酶促降解后的表面形貌揭示了沿深度方向的相结构。研究了PHB解聚酶在PLLA/无规-PHB共混物表面的酶吸附情况。在二元共混物的两个畴上都发现了酶分子。相对于无规-PHB畴,在PLLA畴上发现的酶分子数量更多,这表明该酶对PLLA畴具有更高的亲和力。

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