Dextranase, a hydrolase that specifically hydrolyzes α-1,6-glucosidic bonds, has been used in the pharmaceutical, food, and biotechnology industries. In this study, the strain of Catenovulum agarivorans MNH15 was screened from marine samples. When the temperature, initial pH, NaCl concentration, and inducer concentration were 30 °C, 8.0, 5 g/L, and 8 g/L, respectively, it yielded more dextranase. The molecular weight of the dextranase was approximately 110 kDa. The maximum enzyme activity was achieved at 40 °C and a pH of 8.0. The enzyme was stable at 30 °C and a pH of 5–9. The metal ion Sr2+ enhanced its activity, whereas NH4+, Co2+, Cu2+, and Li+ had the opposite effect. The dextranase effectively inhibited the formation of biofilm by Streptococcus mutans. Moreover, sodium fluoride, xylitol, and sodium benzoate, all used in dental care products, had no significant effect on dextranase activity. In addition, high-performance liquid chromatography (HPLC) showed that dextran was mainly hydrolyzed to glucose, maltose, and maltoheptaose. The results indicated that dextranase has high application potential in dental products such as toothpaste and mouthwash.

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At present, the incidence rate of diabetes is increasing gradually, and inhibiting α-glucosidase is one of the effective methods used to control blood sugar. This study identified new peptides from rice bran fermentation broth and evaluated their inhibitory activity and mechanism against α-glucosidase. Rice bran was fermented with Bacillus subtilis MK15 and the polypeptides of <3 kDa were isolated by ultrafiltration and chromatographic column, and were then subjected to LC-MS/MS mass spectrometry analysis. The results revealed that the oligopeptide GLLGY showed the greatest inhibitory activity in vitro. Docking studies with GLLGY on human α-glucosidase (PDB ID 5NN8) suggested a binding energy of −7.1 kcal/mol. GLLGY acts as a non-competitive inhibitor and forms five hydrogen bonds with Asp282, Ser523, Asp616, and His674 of α-glucosidase. Moreover, it retained its inhibitory activity even in a simulated digestion environment in vitro. The oligopeptide GLLGY could be developed into a potential anti-diabetic agent.

Oligosaccharides have important alimental and medical applications. Dextranase has been used to produce isomalto-oligosaccharides (IMOs). In this study, we isolated dextranase-producing bacteria from sugarcane-cultivated soil. Identification of the isolate based on its phenotypical, physiological, and biochemical characteristics, as well as 16S ribosomal deoxyribonucleic acid gene sequencing yielded Shewanella sp. strain GZ-7. The molecular weight of the dextranase produced by this strain was 100-135 kDa. The optimum temperature and pH for dextranase production were 40 °C and 7.5, respectively. The enzyme was found to be stable at the pH range of 6.0-8.0 and the temperature range of 20 °C-40 °C. Thin-layer chromatography and high-performance liquid chromatography of the enzymolysis products of the substrate confirmed the enzyme to be endodextranase. Under the optimal conditions, the ratio of IMOs could reach 91.8% of the hydrolyzate. The final products were found to efficiently scavenge the 2,2-diphenyl-1-picrylhydrazyl, hydroxyl, and superoxide anion radicals. In general, dextranase and hydrolyzates have high potential prospects for application in the future.

Shrimp paste is one of the traditional foods in eastern China, even in East Asia (Phewpan et al., 2020). The fresh shrimps are fermented naturally by adding high concentration of salt. The fermentation would take over one month normally to form flavor and nutrition (Zhu et al., 2019). Proteases could hydrolysis protein effectively by breaking down the peptide bond that links amino acid to poly-peptide chain, and they account for over half of the total world enzyme markets in the world (