One-Step Partially Purified Lipases (ScLipA and ScLipB) from Schizophyllum commune UTARA1 Obtained via Solid State Fermentation and Their Applications

Abstract

Lipases with unique characteristics are of value in industrial applications, especially those targeting cost-effectiveness and less downstream processes. The aims of this research were to: (i) optimize the fermentation parameters via solid state fermentation (SSF); and (ii) study the performance in hydrolysis and esterification processes of the one-step partially purified Schizophyllum commune UTARA1 lipases. Lipase was produced by cultivating S. commune UTARA1 on sugarcane bagasse (SB) with used cooking oil (UCO) via SSF and its production was optimized using Design-Expert® 7.0.0. Fractions 30% (ScLipA) and 70% (ScLipB) which contained high lipase activity were obtained by stepwise (NH4)2SO4 precipitation. Crude fish oil, coconut oil and butter were used to investigate the lipase hydrolysis capabilities by a free glycerol assay. Results showed that ScLipA has affinities for long, medium and short chain triglycerides, as all the oils investigated were degraded, whereas ScLipB has affinities for long chain triglycerides as it only degrades crude fish oil. During esterification, ScLipA was able to synthesize trilaurin and triacetin. Conversely, ScLipB was specific towards the formation of 2-mono-olein and triacetin. From the results obtained, it was determined that ScLipA and ScLipB are sn-2 regioselective lipases. Hence, the one-step partial purification strategy proved to be feasible for partial purification of S. commune UTARA1 lipases that has potential use in industrial applications.

Synthesis of eicosapentaenoic acid‐enriched medium‐ and long‐chain triglyceride by lipase‐catalyzed transesterification: a novel strategy for clinical nutrition intervention

“…Further, the purification process resulted in a reduction of sn‐2 MCFA content (from 38.70% to 29.35%) and an increase in sn‐2 LCFA content (from 61.30% to 70.65%), in which sn‐2 EPA reached 26.93%. Previous research has indicated that pancreatic lipase is a sn‐1,3‐specific lipase that acts on the sn‐1 or sn‐3 ester bond of the TAG molecule but with significantly lower specificity to EPA at the sn‐1,3 positions compared with other FAs 29,30 . The EPA‐enriched MLCT, where MCFA is predominantly located at the sn‐1,3 positions while EPA is mainly located at the sn‐2 position, could therefore be synthesized to promote absorption of EPA in cases of lipid malabsorption.…”

“…Previous research has indicated that pancreatic lipase is a sn-1,3-specific lipase that acts on the sn-1 or sn-3 ester bond of the TAG molecule but with significantly lower specificity to EPA at the sn-1,3 positions compared with other FAs. 29,30 The EPA-enriched MLCT, where MCFA is predominantly located at the sn-1,3 positions while EPA is mainly located at the sn-2 position, could therefore be synthesized to promote absorption of EPA in cases of lipid malabsorption. Clinical studies showed that the growth in body weight for cancer patients receiving chemotherapy significantly increased when EPA dosage was no less than 2 g d −1 .…”

Clostridium perfringens suppressing activity in black soldier fly protein preparations

“…Fusobacterium nucleatum) (Fischer et al, 2012;Matsue et al, 2019). Lauric acid can be released after lipase digestion of trilaurin, a triglyceride that contains a significant amount of lauric acid (Kam, Woo, & Ong, 2017). However, the results showed that BTD did not significantly (p < 0.05) inhibit the growth of C. perfringens (Fig.…”