Journal
MACROMOLECULES
Volume 39, Issue 17, Pages 5789-5795Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ma060908v
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A new core- sheath structure constructed by two kinds of molecular conformationss2/1 helix (alpha-form) and planar zigzag (beta-form) conformationssin biodegradable poly[(R)-3-hydroxybutyrate] (P(3HB)) fiber was revealed by 0.5 mu m microbeam X- ray diffraction in synchrotron radiation. P( 3HB) fiber processed by a method combining cold- drawing and two- step- drawing has both beta- form and,- form molecular chains in the core region, while the sheath region consists of only beta- form chains. The crystallinity and orientation of beta- form crystals in the core region were higher than those in the sheath region. Microbeam X- ray diffraction during two- stepdrawing of cold- drawn fiber at room temperature revealed the generation mechanism of this interesting coresheath structure at the highly ordered structural level. The,- form in core region was generated from amorphous chains between beta- form lamellar crystals by the strong stretching of two- step- drawing. However, in the sheath region, since the beta- form lamellar crystals rotated along the two- step- drawing direction, molecular chains between lamellar crystals could not elongate sufficiently. The enzymatic degradation of P(3HB) fibers was performed with an extracellular poly( hydroxybutyrate) depolymerase purified from Ralstonia pickettii T1. The intensity of a reflection derived from the, beta- form decreased faster than that of the beta-form in X- ray fiber diagram, despite the, beta- form existing in the core region. The enzymatic degradation progressed from ( 1) the amorphous chains between alpha- form lamellar crystals in the sheath region, ( 2) the, beta-form molecular chains in the core region, and ( 3) the alpha- form lamellar crystals in the whole fiber. The result that the rate of enzymatic erosion of the, beta- form was faster than that of the alpha- form indicates that the rate of enzymatic degradation can be controlled by the molecular conformation, despite the same chemical structure.
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