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   <subfield code="a">Enzymatic Degradation and Aminolysis of Microbial Poly(3-hydroxybutyrate- co -4-hydroxybutyrate) Single Crystals</subfield>
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   <subfield code="c">[Wen-chuan Hsieh, Hiroshi Mitomo, Ken-ichi Kasuya, Tadashi Komoto]</subfield>
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   <subfield code="a">Solution-grown single crystals of poly(3-hydroxybutyrate-co-4-hydroxybutyrate) [P(3HB-co-4HB)] were hydrolyzed by polyhydroxybutyrate (PHB) depolymerase from Ralstonia pickettii T1. Enzymatic degradation proceeded from the edges of lamellar crystals, yielding serrated contour and small crystal fragments. Gel permeation chromatography analysis revealed that the molecular weights of the crystals decreased during enzymatic degradation, suggesting that the enzymatic hydrolysis of chain-folding regions at the crystal surfaces occurred in addition to the enzymatic degradation at crystal laterals or edges. After P(3HB-co-4HB) single crystals were aminolysed in 20% aqueous methylamine solution to remove the folded-chain regions and enzymatic degradation by lipase from Rhizopus oryzae to remove 4HB components at crystal surfaces of single crystal aminolyzed, it was found that a small amount (up to ca. 2mol%) of 4HB component can be incorporated into the P(3HB) mother crystal lattice irrespective of the 4HB content.</subfield>
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