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Purpose: This study was conducted for comparison of clinical and second look arthroscopic results between early and delayed reconstruction of acute anterior cruciate ligament (ACL) injuries. Materials and Methods: Thirty-six patients who underwent ACL reconstruction between March 2008 and October 2011 were enrolled in this study. We divided the patients into two groups, those in the early reconstruction group underwent surgery before one week, and those in the delayed reconstruction group underwent surgery after three weeks, before six weeks. We checked clinical results and second look arthroscopic results and analyzed correlation of clinical and second look arthroscopic results. Results: At the final follow up, the Lysholm, International Knee Documentation Committee, and Tegner score were not statistically different between the two groups (p=0.173, p=0.154, p=0.109). No difference for the range of motion (p=0.808, p=0.680), Lachman test (p=0.377), and pivot shift test (p=0.894) was observed between the groups. In the results of second look arthroscopy, there was no difference in graft continuity (p=0.936), tension (p=0.944) and synovial coverage (p=0.789). No statistical clinical correlation was observed between clinical and second look arthroscopic results (p>0.05). Conclusion: We obtained satisfactory clinical and second look arthroscopic results in both the early and delayed ACL reconstruction groups. Therefore, early reconstruction of ACL performed before one week could be a treatment options for acute ACL injury.

Results: The volume of blood loss during the operation was statistically lesser in the PFNA group (P

The gene (bglT) encoding Tca beta-glycosidase (Thermus caldophilus GK24 beta-glycosidase) was overexpressed under the control of the trp promoter on a high-copy-number plasmid, pTRPES, in Escherichia coli W3110. The purified Tca beta-glycosidase enzyme was used in a galactosyl-transfer reaction to synthesize galacto-oligosaccharides from lactose. The optimum temperature and pH for the enzyme to synthesize galacto-oligosaccharides from 30% (w/v) lactose were 80 degrees C and 6.0, respectively. The major product of the reaction was a trisaccharide. The thermostable Tca beta-glycosidase produced galacto-oligosaccharides efficiently during the hydrolysis of lactose.

A peptide corresponding to the 23 N-terminal residues of αs1-casein, αs1(1-23), was purified from a peptic hydrolyzate of αs1-casein. The emulsifying activity of αs1(1-23) varied depending on the concentration. When the concentration was higher than 2%, αs1(1-23) showed a similar emulsifying activity to αs1-casein in neutral pHs. The emulsion capacity of αs1(1-23) was about one half that of αs1-casein. The extent of adsorption of αs1(1-23) onto the oil globule surface was markedly high. In the acidic pH region (pH 5.5 – 3.0), αs1(1-23) maintained a high emulsifying activity, whereas αs1-casein lost its emulsifying activity. These results suggest that αs1(1-23) acts as an emulsifying agent and probably can be used in some foods such as processed cheese or fermented milk products.

The pH 4.6-soluble fraction of the peptic hydrolyzate of as 1-casein contained the 23 N-terminal residues, αsl-CN(fl-23), as a major pep-tide. Reversed-phase HPLC indicated that small amounts of other peptides such as αsl-CN(f154-199) were also contained in this fraction. By removing of these peptides, the emulsifying activity (EA) of the αsl-CN(fl-23) fraction was markedly decreased. However, when the removed peptide fraction was added to the purified αsl-CN(fl-23), the EA was increased. Some synergistic effect in the emulsification seemed to exist between αsl-CN(fl-23) and the other peptides. Although the purified αsl-CN(fl-23) had low EA values at neutral pH levels, it showed high emulsifying and surface activities in the acidic pH region.

A hydrophobic peptide of 17 residues, β-CN (f193—209), and a hydrophilic peptide of 25 residues, β-CN (f1 ~ 25), were isolated from enzyme hydrolyzates of bovine β-casein. The emulsifying activity (EA) of both peptides was low at a neutral pH. In the acidic or alkaline condition, however, β-CN (f 193 — 209) showed high EA values. β-CN (f1 ~ 25) also showed high EA values at acidic pHs. These peptides are shown to be more surface active at pH 3 than at pH 7.

β-CN(f193–209), a hydrophobic peptide of 17 residues obtained from the chymosin hydrolyzate of β-casein, had little emulsifying activity (EA) at a neutral pH. When mixed with a hydrophilic glycomacropeptide (GMP) derived from κ-casein however, the EA of β-CN(f193-209) increased greatly. The mixing ratio of the peptides affected the EA as well as the adsorption of the peptides to oil droplets. Scanning electron microscopy indicated that the peptide film surrounding the emulsified oil droplets was thick and rough compared to the protein film. An amphipathic structure formed by some interaction between the hydrophilic GMP and the hydrophobic β-CN(f193-209) might contribute to the formation of the thick peptide film and stabilize the emulsified oil.