微生物絮凝剂生产菌T1的鉴定及其对生活污水絮凝特性

从活性污泥中分离筛选絮凝剂产生菌,得到一株对高岭土悬浊液具有较高絮凝活性的微生物絮凝菌T1.根据菌株的生理生化鉴定以及16S r DNA基因序列分析,确定该菌株为芽孢杆菌(Bacillus sp),该菌的絮凝活性物质分布在发酵液上清液中.通过正交实验确定最佳生活污水絮凝条件为絮凝剂投加量5%,污水p H值7.0,助凝剂Ca Cl2投加量为2%,在此条件下,T1发酵上清液对生活污水的絮凝率为83.85%.     

The oligopeptides production by the feather-degrading bacterium Bacillus methylotrophicus H0北大核心CSCD

Due to the high nutritive value of oligopeptides and the waste of feather resources, this study aimed at screening efficient strains of bacteria able to rapidly degrade feathers and produce large quantities of value-added oligopeptides. In order to assess the potential yield of oligopeptides, the promising strain H0 was selected from 16 feather-degrading microorganisms. To identify the strain, we analyzed the morphological and physiological characteristics of different strains, and carried out a gene sequence analysis of their 16S rRNAs. A single factor experiment was used to promote feather degradation and oligopeptide production, and the characteristics of the oligopeptides produced were also analyzed by Liquid Chromatography-Tandem Mass Spectrometry (LC-MS/MS). The strain was identified as Bacillus methylotrophicus. The optimal initial pH and temperature for oligopeptide production were 11 and 40 °C, respectively. After 72 h of fermentation under these optimal conditions, the feathers were almost completely degraded, with a 38.19% of oligopeptides (accounting for 67.53% of the total soluble peptides) and a 11.11% of free amino acids produced. LC-MS/MS analysis indicated that the oligopeptides were mainly short peptides containing 5-10 amino acids, with a molecular mass (Mr) of less than 1 300. Moreover, the peptides were abundant in branched-chain amino acids, that might be responsible for the antioxidant property of the feather hydrolysate. Our results demonstrate the great capability of B. methylotrophicus H0 in feather degradation and oligopeptide production. This research provides a high-quality microorganism resource, and the scientific basis for the development of feather-derived oligopeptide products. © 2018 Science Press. All rights reserved.