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.
Isolate VT11 is a fungal cellulolytic isolated from vermicomposting oil palm empty fruit bunch (OPEFB). Isolate VT11 has a cellulolytic activity index of 1.0 on 1% CMC, but this isolate has never been used to produce cellulase from coffee pulp waste. The coffee pulp consists of organic components with the highest cellulose content (63%) so that it can be used as a substrate for cellulase production by fungal cellulolytic under solid-state fermentation (SSF). This study aims to know the potential of isolate VT11 as a candidate for cellulase producer. The potential of isolate VT11 as a candidate for cellulase producer was known by the cellulase activity on coffee pulp waste under solid-state fermentation. After that, cellulase was characterized by pH optimization and stabilization. Cellulase production was done by inoculating isolate VT11 in 10 g solid substrate of coffee pulp. The result shows that the isolate VT11 can potentially produce cellulase with the highest enzyme activity of 1.857 U/mL after 96 hours of incubation at 30 °C. Cellulase from isolate VT11 is optimal at pH 4.5 and stable at pH 5-6.5. Based on this result, it is suggested that the isolate VT11 can be used for cellulase production using coffee pulp waste as substrate agro-industrial residues. Further investigation such as species identification of isolate VT11, purification, and characterization of cellulase produced by isolate VT11 was needed.
Lignoselulosa merupakan penyusun utama dinding sel tumbuhan, sehingga keberadaannya berlimpah di alam. Aktinomiset indigenous yang memiliki aktivitas selulolitik dan xilanolitik ekstraseluler berpeluang sebagai agens biokonversi limbah berlignoselulosa menjadi produk bermanfaat. Penelitian ini bertujuan untuk mendapatkan aktinomiset potensial yang memiliki aktivitas selulolitik dan xilanolitik. Penelitian ini diawali dari isolasi dan pemurnian aktinomiset indigenous asal lahan perkebunan kelapa sawit dan Taman Nasional Bukit Duabelas Jambi.Tahapan selanjutnya adalah penapisan aktivitas selulolitik dan xilanolitik dari aktinomiset, uji pertumbuhan aktinomiset pada mikrokristalin selulosa, dan identifikasi aktinomiset potensial berdasarkan karakter morfologi, fisiologi dan biokimia. Hasil penelitian menunjukkan bahwa aktinomiset isolat S2 yang diisolasi dari lahan perkebunan kelapa sawit mempunyai aktivitas selulolitik dan xilanolitik lebih baik dari keempat isolat lain. Aktinomiset isolat S2 juga mampu tumbuh secara lebih baik pada mikrokristalin selulosa. Aktivitas selulolitik, xilanolitik dan kemampuan tumbuh pada mikrokristalin selulosa dari aktinomiset isolat S2 menunjukkan potensinya sebagai agens pendegradasi material belignoselulosa. Berdasarkan identifikasi morfologi, fisiologi dan biokimia, aktinomiset isolat S2 tergolong dalam genus Streptomyces.
Enam puluh juta ton amilum per tahun di Indonesia memiliki nilai jual yang rendah berdasarkan nilai ekonomi skala internasional. Peningkatan pemanfaatan amilum dapat dilakukan dengan menghidrolisis amilum menjadi glukosa secara enzimatik oleh mikrob amilolitik. Yeast amilolitik memiliki pertumbuhan yang lebih cepat, lebih efektif memecah amilum dari kapang dan dapat digunakan sebagai protein sel tunggal. Penelitian ini bertujuan untuk mendapatkan isolat yeast amilolitik yang berasal dari buah sukun, buah pisang, buah mangga dan buah durian. Hasil isolasi didapatkan 11 isolat yeast. Uji semikuantitatif dengan media SSA terhadap 11 isolat yeast, terdapat 5 isolat yang bersifat amilolitik yaitu isolat SiJi-P3, SiJi-P5, SiJi-S1, SiJi-S2, dan SiJi-M2. Isolat SiJi-P3 dan SiJi-P5 yang teridentifikasi sebagai Saccarhomyceteae mempunyai indek amilolitik terbesar.
The human body does not have an enzyme that can break down uric acid, so the accumulation of uric acid can cause disease. This problem can be overcome by uricolytic therapy by utilizing the activity of the uricase enzyme. In this study, the uricase enzyme was extracted from goat liver by optimizing the centrifugation speed and the extraction pH. The purpose of the optimization is to get maximum uricase activity. Uricase extraction to optimize centrifugation speed using borate buffer pH 8.5 then centrifuged at 7.000; 9.000; 11.000; 13.000 and 15.000 rpm with a temperature of 4oC. Furthermore, pH optimization was carried out using pH buffers 6, 7, 8, 9, 10 and 11 by centrifuging the optimum speed obtained. The crude extract obtained was further tested for its enzyme activity . The results showed that the highest uricase activity was achieved if the extraction was carried out at pH 8 using centrifugation at an optimum speed of 13,000 rpm. The higher uricase activity indicates that the extracted uricase concentration is increasing.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.