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Using tricaprylin (TC) and trilinolenin (TLN) as substrates, biosynthesis of medium-long-medium (MLM) type structured lipids (SLs), by Lipozyme IM from Rhizomucor meihei and Novozym 435 from Candida antarctica , was investigated to determine their capacity as biocatalysts for the biosynthesis of SLs. At 30°C, Lipozyme IM showed higher bioconversion yield (24.7%) and initial enzyme activity (6.3 mumol CLnC/g enzyme/min) as compared to that of 24.0% and 1.6 mumol CLnC/g enzyme/min, respectively, for the Novozym 435 at 50°C. As a result, Lipozyme IM was subsequently used for further investigations. The SLs were recovered and characterized by silver-ion exchange high-performance liquid chromatography and gas-liquid chromatography. The structural analyses indicated that the major products of the enzymatic reaction were 1,3-dicapryl-2-linolenyl glycerol (CLnC) and 1(3)-capryl-2,3(1)-dilinolenyl glycerol (CLnLn). In order to optimize the bioconversion yield of CLnC, selected parameters, including initial water activity and solvent type, lipase concentration (5 to 20 mg solid enzyme), substrate molar ratios (TC:TLN of 1:4 to 8:1) and molecular sieve (5 to 20 mg/mL, Type 3A), were investigated. The experimental results showed that using hexane at initial aw 0.06, 10 mg solid enzyme/mL and substrate molar ratio of TC to TLN of 6:1 resulted in the highest bioconversion yield of 73.2% of CLnC. However, the addition of molecular sieve to the reaction medium resulted in a 14.0% decrease in the bioconversion yield of CLnC. Using the optimized conditions, the effects of TLN concentration and other selective limiting parameters, including the denaturation of enzyme, aw and the formation of glycerol layer, on the mass productivity (PM), enzymatic productivity (PE) and volumetric productivity (PV) of the interesterification reaction were investigated. Using 80 mM TLN, the maximum PM of 15.5 mg CLnC/g substrates/h was obtained; however, using 200 mM TLN, the maximum PE and PV were 0.07 mg/enzyme unit/h and 6.1 g CLnC/L/h, respectively. The addition of 3 mg Silica gel to the reaction medium resulted in 52.0, 37.3 and 37.3% increase in PM, PE and PV, respectively.

Separation-individuation has been consistently identified as a critical process in adolescent development. Dysfunction in the separation-individuation process has previously been linked to pathology among college students and adults. The purpose of this study was to validate the psychometric integrity of the Dysfunctional Separation-Individuation Scale in a population of young adolescents. A one factor structure of the 19-item scale was obtained. The scale correlated highly in the expected directions with other measures of separation-individuation, as well as with measures of depression and positive adaptation. / Department of Educational Psychology

Modulation of cell adhesion is essential to the cell rearrangements that characterize Xenopus gastrulation. The spatial and temporal regulation of cell movement requires a highly coordinated cross-talk between cadherin and integrin adhesion receptors. Beta-parvin is an integrin associated scaffolding protein consisting of two calponin homology (CH) domains. Xenopus beta-parvin is highly conserved being ~95% similar to mammalian orthologs. Beta-parvin is expressed in the blastocoel roof and dorsal marginal zone of the embryo during gastrulation, suggesting a potential role in morphogenesis. Over-expression of full-length beta-parvin has no effect on embryogenesis, however, over-expression of either CH domain causes a failure in gastrulation. When over-expressed the CH1 domain causes a failure in fibronectin (FN) matrix assembly, epiboly and convergent extension in vivo. CH1 domain over-expression also inhibits tissue separation (TS) and Brachet’s cleft formation. The CH1 domain of beta-parvin localizes to sites of cell-cell adhesion, and down-regulates C-cadherin adhesion through activation of Rac1, independent of receptor expression. Significantly, the CH1 domain can rescue convergent extension downstream of integrin ex vivo suggesting a role for beta-parvin in the integrin mediated control of cell intercalation. Over-expression of the CH2 domain also inhibits morphogenesis in a similar fashion as CH1. However, the CH2 domain localizes to sites of integrin adhesion and inhibits integrin function resulting in a loss of FN assembly. The CH2 domain binds ILK and inhibits integrin function. When over-expressed the CH2 domain promotes TS in the pre-involution mesoderm through the activation of Rho. While the CH1 domain inhibits TS through Rac and the CH2 domain promotes TS through Rho, full-length beta-parvin over-expression has no embryonic phenotype and its signaling properties appear to be intermediate between expression of either isolated CH domain. At the dorsal lip full-length beta-parvin shuttles between integrin in the pre-involution mesoderm and cell-cell adhesion sites in the post-involution mesoderm indicating it plays significant roles in the previously characterized integrin-cadherin cross talk. My research has defined novel roles for beta-parvin as a key player in the regulation of integrin-cadherin cross-talk during tissue morphogenesis.