The community-based approach to health research and intervention is a model of inquiry rooted in Freire's participatory action research (PAR). We need to show, in concept and practice, what it is about PAR that may be well suited for the types of health issues we encounter in inner-city environments. What type of learning results, how does this respond to particular health issues in the urban context, and what are the particular challenges faced in translating Freire's model into today's urban setting?To investigate these questions, we describe a recent PAR project in Southeast Los Angeles, California-an area known to some as "Asthmatown." One salient finding of the research is that PAR allows the integration of complex and multiple forms of knowledge, and this is a necessary response to the complex and multiplex nature of cumulative impacts. There are challenges to translating the model to the urban setting, however, such as the difficulties of participation in today's urban milieu. The research leads to some lessons for practitioners, such as the need to build "constant" elements into PAR projects. Lastly, we reflect on implications of this model for institutional reform.

Summary: Two different types of biodegradable polyester composites, PLLA fiber‐reinforced PCL and PCL/PLLA blend films were prepared at PCL/PLLA ratio of 88/12 (w/w), together with pure PCL and PLLA films. Their enzymatic degradation was investigated by the use of Rhizopus arrhizus lipase and proteinase K as degradation enzymes for PCL and PLLA chains, respectively. In the FRP film, the presence of PLLA fibers accelerated the lipase‐catalyzed enzymatic degradation of PCL matrix compared with that in the pure PCL film, whereas in the blend film, the presence of PLLA chains dissolved in the continuous PCL‐rich domain retarded the lipase‐catalyzed enzymatic degradation of PCL chains. In contrast, in the FRP film, the proteinase K‐catalyzed enzymatic degradation of PLLA fibers was disturbed compared with that of the pure PLLA film, whereas in the blend film, the proteinase K‐catalyzed enzymatic degradation rate of particulate PLLA‐rich domains was higher than that of pure PLLA film. The reasons for aforementioned enhanced and disturbed enzymatic degradation are discussed.Normalized PCL weight loss of pure PCL, FRP, and blend films as a function of Rhizopus arrhizus lipase‐catalyzed enzymatic degradation time.magnified imageNormalized PCL weight loss of pure PCL, FRP, and blend films as a function of Rhizopus arrhizus lipase‐catalyzed enzymatic degradation time.

The enzymatic degradation of poly(L-lactic acid) (PLLA) fibers with different low draw ratios (1.0, 1.2, and 1.4 times) was investigated in tris-HCl buffer solution (pH ¼ 8.6) with proteinase K by the use of gravimetry, scanning electron microscopy (SEM), gel permeation chromatography (GPC), differential scanning calorimetry (DSC), and tensile testing. Surprisingly, even the small drawings (1.2 and 1.4 times) disturbed the proteinase K catalyzed enzymatic degradation of the PLLA fibers. This should have been because the enzyme could not attach to the extended (strained) chains in the amorphous regions of the uniaxially oriented PLLA fibers or could not catalyze the cleavage of the strained chains. The accumulation of crystalline residues formed as a result of selective cleavage, and removal of the amorphous chains was not observed, even for as-spun PLLA fibers. This indicated the facile release of formed crystalline residues from the surface of the as-spun PLLA fibers during enzymatic degradation. Such release may have been because the crystalline regions of the as-spun PLLA fibers were oriented with their c axis parallel to the machine direction, as reported for biaxially oriented PLLA films. Gravimetry, SEM, and tensile testing could trace the enzymatic degradation of the PLLA fibers, although the enzymatic degradation of the PLLA fibers was untraceable by GPC and DSC.

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