NCIM Resource Center, National Chemical Laboratory (CSIR), Pune 411008, Maharashtra, India.
Bioresour Technol. 2011 Jun;102(11):6569-72. doi: 10.1016/j.biortech.2011.01.014. Epub 2011 Jan 14.
Mutants of Penicillium janthinellum NCIM 1171 were evaluated for cellulase production using both submerged fermentation (SmF) and solid state fermentation (SSF). Mutant EU2D-21 gave highest yields of cellulases in both SmF and SSF. Hydrolysis of Avicel and cellulose were compared using SmF and SSF derived enzyme preparations obtained from EU2D-21. Surprisingly, the use of SSF derived preparation gave less hydrolysis compared to SmF derived enzymes. This may be due to inactivation of β-glucosidase at 50°C in SSF derived enzyme preparations. SmF derived enzyme preparations contained both thermostable and thermosensitive β-glucosidases where as SSF derived enzyme preparations contained predominantly thermosensitive β-glucosidase. This is the first report on less thermostability of SSF derived β-glucosidase which is the main reason for getting less hydrolysis.
青霉菌 NCIM 1171 的突变体被评估了在深层发酵（SmF）和固态发酵（SSF）条件下的纤维素酶的生产能力。突变体 EU2D-21 在 SmF 和 SSF 中均产生了最高量的纤维素酶。用 SmF 和 SSF 从 EU2D-21 中获得的酶制剂对微晶纤维素和纤维素进行了水解比较。令人惊讶的是，与 SmF 衍生酶相比，使用 SSF 衍生酶制剂的水解效率更低。这可能是由于 SSF 衍生酶制剂中β-葡萄糖苷酶在 50°C 下失活。SmF 衍生酶制剂中含有热稳定和热敏β-葡萄糖苷酶，而 SSF 衍生酶制剂中主要含有热敏β-葡萄糖苷酶。这是关于 SSF 衍生β-葡萄糖苷酶的热稳定性降低的首次报道，这是水解效率降低的主要原因。
