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CONTEXT: Diet quality is directly related to glycemic control in individuals with type 2 diabetes mellitus (T2DM). The use of dietary indices can provide a comprehensive understanding of the relationship between diet quality and clinical outcomes. OBJECTIVE: The aim was to evaluate the relationship between diet quality, measured using dietary indices, and its impact on improving glycemic control in individuals with T2DM through health interventions. DATA SOURCE: This study was conducted using 6 databases, including Web of Science, MEDLINE (via PubMed), Embase, Bireme, Scopus, and Cumulative Index to Nursing and Allied Health Literature (CINAHL), as well as the gray literature (Google Academic). DATA EXTRACTION: Randomized clinical trials that evaluated the effectiveness of health interventions in adult and older adult individuals with T2DM and presented data on diet quality evaluated using dietary indices and the percentage of glycated hemoglobin (%HbA1c) were included. DATA ANALYSIS: A total of 3735 articles were retrieved, 4 of which were included in the study selection stages. The quality indices assessed in the studies were the Alternate Healthy Eating Index (AHEI), Healthy Eating Index-2010 (HEI-2010), Diet Quality Index-International (DQI-I), and Diet Quality Index-Revised (DQI-R). A reduction in %HbA1c was observed in 2 studies, which correlated with the AHEI and DQI-I scores in the intervention groups. The approach of using food labels to improve diet quality reduced %HbA1c by 0.08% in the intervention group compared with the control group. Only 1 study found no significant association between the DQI-R index and %HbA1c. Additionally, negative correlations were observed between body weight and the AHEI and DQI-I scores. CONCLUSION: Health interventions improved diet quality, glycemic control, and weight loss in individuals with T2DM. SYSTEMATIC REVIEW REGISTRATION: PROSPERO no. CRD42023430036.
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BACKGROUND: The Bacillus subtilis endo-ß-1,4-glucanase (BsCel5A) hydrolyzes ß-1,3-1,4-linked glucan, and the enzyme includes a family 3 carbohydrate-binding module (CBM3) that binds ß-1,4-linked glucan. METHODS: Here we investigate the BsCel5A ß-1,3-1,4 glucanase activity after exchanging the CBM3 domain for the family 11 CBM from Ruminiclostridium thermocellum celH (RtCBM11) having ß-1,3-1,4 glucan affinity. RESULTS: The BsCel5A-RtCBM11 presents a 50.4% increase in Vmax, a 10% reduction in K0.5, and a 2.1-fold increase in catalytic efficiency. Enzyme mobility and binding to barley ß-1,3-1,4 glucan and pre-treated sugarcane bagasse were investigated using Electron Paramagnetic Resonance (EPR) with Site-Directed Spin Labeling (SDSL) of the binding site regions of the CBM3 and RtCBM11 domains in the BsCel5A-CBM3 and BsCel5A-RtCBM11, respectively. Although higher mobility than the RtCBM11 was shown, no interaction of the spin-labeled CBM3 with ß-1,3-1,4 glucan was observed. In contrast, a Ka value of 0.22 mg/mL was estimated from titration of the BsCel5A-RtCBM11 with ß-1,3-1,4 glucan. Enzyme binding as inferred from altered EPR spectra of the BsCel5A-RtCBM11 was observed only after xylan or lignin extraction from sugarcane bagasse. Binding to xylan- or lignin-free lignocellulose was correlated with a 4.5- to 5-fold increase in total reducing sugar release as compared to the milled intact sugarcane bagasse, suggesting that xylan impedes enzyme access to the ß-1,3-1,4 glucan. CONCLUSIONS: These results show that the non-specific binding of the BsCel5A-RtCBM11 to the lignin component of the cell wall is minimal, and represent the first reported use of EPR to directly study the interaction of glycoside hydrolyse enzymes with natural insoluble substrates.