Chryseobacterium carnipullorum 9_R23581^T, isolated from raw chicken meat, was evaluated for its potential to degrade keratin found in feathers. The focus of this study was to heterologously express and characterise a keratinolytic enzyme produced by C. carnipullorum. Chryseobacterium carnipullorum secretes proteolytic enzymes that have feather degrading capabilities during its exponential growth phase. This study concluded that the most likely main component of the keratinolytic enzymes of C. carnipullorum was peptidase M64, a serine-endopeptidase with a molecular weight in crude form of 49.46 kDa. Primers were designed on the selected gene of interest, which was amplified from the genome of C. carnipullorum (accession number NZ-FRCD01000002.1). The gene coding for peptidase M64 was further cloned, propagated and expressed in E. coli BL21 [DE3] cells. Purification was by Immobilised Metal Affinity Chromatography (IMAC). The molecular weight of the keratinase was about 50 kDa after purification while its optimum temperature and pH were 50 °C and 8.5, respectively. The activity of this keratinase was inhibited by phenylmethylsulfonyl fluoride (PMSF) and it was enhanced by the presence of divalent metal ions such as Mg²⁺ and Ca²⁺. Enzyme activity was further assayed by application to chicken feathers and observed degradation was an indication of keratinolytic potential.

从生鸡肉中分离出的Chryseobacterium carnipullorum 9_R23581 ^{T对其降解羽毛中角蛋白的潜力进行了评估。}本研究的重点是异源表达和表征由C. carnipullorum 产生的角质分解酶。Chryseobacterium carnipullorum分泌蛋白水解酶，在其指数生长期具有降解羽毛的能力。该研究得出结论认为，肉苁蓉角蛋白分解酶最可能的主要成分是肽酶 M64，它是一种粗制形式的分子量为 49.46 kDa 的丝氨酸内肽酶。在选定的感兴趣基因上设计引物，该基因从C. carnipullorum的基因组中扩增(登录号 NZ-FRCD01000002.1)。编码肽酶 M64 的基因被进一步克隆、繁殖并在大肠杆菌BL21 [DE3] 细胞中表达。通过固定化金属亲和色谱法(IMAC)进行纯化。纯化后角蛋白酶的分子量约为50 kDa，其最适温度和pH分别为50°C和8.5。该角蛋白酶的活性受到苯甲基磺酰氟(PMSF)的抑制，而二价金属离子如Mg ²⁺和Ca ²⁺的存在增强了该活性。通过应用于鸡毛进一步测定酶活性，观察到的降解是角质溶解潜力的指示。