Polysaccharides rich coffee pulp is one of some abundant agricultural waste in Indonesia. The pulp also contains protein which may lead to be an important source for industrial bioprocessing. Under solid-state fermentation (SSF) by Pestalotiosis sp VM9 using of this pulp, reducing sugar was produced 392.35 μg/ml after 6 days incubation at 30°C. Meanwhile, SSF of the pulp by Aspergillus sp. VTM5, after 5 days of incubation 446.6 µg/ml of reducing was released. The investigation proved that the hydrolyzates medium which were produced under SSF by Pestalotiosis sp VM9 and Aspergillus sp. VTM5 can be used as a source for single cell protein (SCP) Saccharomyces cerevisiae production. The SCP productions using both hydrolyzates were1.89x106 2.9x106 cell/mL after 54 and 48 hours of incubation at 30°C. Furthermore, during SCP production, S. Cerevisiae consumed sugars as carbon sources in a range of 189.8-225.5 μg/ml (49.5-51.6%) from initial concentration. From the results, it is suggested that the coffee pulp waste can be used as a cheap medium for SCP production. Further investigation to improve SCP production efficiency, optimizing of hydrolysis under SSF and analysis of hydrolyzates component were needed.
Coffee pulp biomass waste can easily be found anywhere in Indonesia, considering it is the fourth world's largest coffee exporter. The utilization of coffee pulp is very limited and is categorized as a source of pollutants in water bodies and soils. In contrast, coffee pulp waste is very potential because 63% of the main compound is cellulose. Microbial utilization of this waste for enzyme production purposes, especially cellulase, is a breakthrough that may lead to reduce production costs. Initial investigations showed that Aspergillus sp. VTM1 through solid-state fermentation (SSF) could produce cellulases. Optimal cellulase could be produced if 10 g coffee pulp with 10% moisture is inoculated using 108 spores/mL of Aspergillus sp. VTM1 for 48 hours at 30 °C. Hydrolysis of 1% carboxymethyl cellulose (CMC) substrate in 50 mM acetate buffer pH 5 by this cellulase showed that the enzyme activity reached up to 1.18 U/mL. The optimum pH of the enzyme was 5 and stable at 3-3.5 and 4-7. The success of the first step of this investigation will be a cheap way of producing cellulases.
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