Background: Unlike the ␣-helix/␤-strand, the non-regular region contains amino acid defined as disordered residue (DR); its effect on enzyme structure and function is elusive. Results: Terminal DR deletions significantly increased xylanase thermostability and activity. Conclusion: Terminal DRs disturb xylanase thermostability and activity. Significance: DR deletion increased regular secondary structural content, and hence, led to slow decreased ⌬G 0 in the thermal denaturation process, and ultimately, enhanced enzyme thermostability.

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BACKGROUND Oil bodies (OBs) are a kind of natural and stable oil nucleate microcapsule in which the triglyceride matrix can be used as an appropriate carrier of hydrophobic molecules. Astaxanthin has high antioxidant properties but is extremely sensitive to oxidation, causing the loss of its bioactive properties. RESULTS The purpose of this study was to clarify the effects of environmental factors (light, oxygen, temperature, and pH) on the physical and oxidative stability of astaxanthin microcapsules prepared with peanut oil bodies (POBs). After 14 days of storage, the retention rate of astaxanthin in peanut oil microcapsules (POMs) was significantly increased. The astaxanthin retention rate of POMs stored under light conditions was higher than under dark conditions. Similarly, the retention rate of astaxanthin in POMs was significantly increased during vacuum storage. The astaxanthin retention rate was also the highest when POMs were stored at 4 °C, whereas it was the lowest at pH 3.0. CONCLUSION The experiment demonstrated that microcapsulation could improve the astaxanthin retention rate and storage stability, and recombinant OBs were potential ideal wall materials for astaxanthin embedding. © 2022 Society of Chemical Industry

The Aspergillus niger xylanase (Xyn) was used as a model to investigate impacts of un-structured residues on GH11 family enzyme, because the β-jelly roll structure has five residues (Ser1Ala2Gly3Ile4Asn5) at N-terminus and two residues (Ser183Ser184) at C-terminus that do not form to helix or strand. The N- or/and C-terminal residues were respectively deleted to construct three mutants. The optimal temperatures of XynΔN, XynΔC, and XynΔNC were 46, 50, and 46°C, and the thermostabilities were 15.7, 73.9, 15.5 min at 50°C, respectively, compared to 48°C and 33.9 min for the Xyn. After kinetic analysis, the substrate-binding affinities for birch-wood xylan decreased in the order XynΔC>Xyn>XynΔNC>XynΔN, while the Kcat values increased in the order XynΔC