Access the full text.
Sign up today, get DeepDyve free for 14 days.
Purpose The present study aimed to explore the binding ability of acyl-CoA binding protein 2 to fatty acid acyl-CoA esters and its effect on Monascus pigment production in M. ruber CICC41233. Methods The Mracbp2 gene from M. ruber CICC41233 was cloned with a total DNA and cDNA as the templates through the polymerase chain reaction. The cDNA of the Mracbp2 gene fragment was ligated to expression vector pGEX-6P-1 to construct pGEX-MrACBP2, which was expressed in Escherichia coli BL21 to obtain the fusion protein GST-MrACBP2 and then measure the binding ability of fatty acid acyl-CoA esters. Additionally, the DNA of the Mracbp2 gene fragment was ligated to expression vector pNeo0380 to construct pNeo0380-MrACBP2, which was homolo- gously over-expressed in M. ruber CICC41233 to evaluate Monascus pigment production and fatty acid. Results The cloned Mracbp2 gene of the DNA and cDNA sequence was 1525 bp and 1329 bp in length, respectively. The microscale thermophoresis binding assay revealed that the purified GST-Mr ACBP2 had the highest affinity for palmitoyl-CoA (Kd =70.57 nM). Further, the Mracbp2 gene was homologously overexpressed in M. ruber CICC41233, and a positive transformant M. ruber ACBP-E was isolated. In the Monascus pigments fermentation, the expression level of the Mracbp2 gene was increased by 1.74-fold after 2 days and 2.38-fold after 6 days. The palmitic acid con- tent and biomass in M. ruber ACBP2-E were significantly lower than that in M. ruber CICC41233 on 2 days and 6 days. However, compared with M. ruber CICC41233, the yields of total pigment, ethanol-soluble pigment, and water-soluble pigment in M. ruber ACBP2-E increased by 63.61%, 71.61%, and 29.70%, respectively. Conclusions The purified fusion protein GST-Mr ACBP2 exhibited the highest affinity for palmitoyl-CoA. The Mracbp2 gene was overexpressed in M. ruber CICC41233, which resulted in a decrease in palmitic acid and an increase in Monascus pigments. Overall, the effect of Mr ACBP2 on the synthesis of fatty acid and Monascus pigment was explored. This paper explored the effect of Mr ACBP2 on the fatty acid synthesis and the synthesis of Monascus pig- ment. The results indicated the regulation of fatty acid synthesis could affect Monascus pigment synthesis, providing a novel strategy for improving the yield of Monascus pigment. Keywords Acyl-CoA binding protein, M. ruber CICC41233, Mracbp2 gene, Affinity, Monascus pigments Jingjing Cui and Mengmeng Liu equally contributed to the manuscript. of China Jiangxi Key Laboratory of Organic Chemistry, Jiangxi Science *Correspondence: and Technology Normal University, Nanchang 330013, People’s Republic Chuannan Long of China email@example.com School of Life Science, Jiangxi Science & Technology Normal University, Bin Zeng Nanchang 330013, People’s Republic of China firstname.lastname@example.org Jiangxi Key Laboratory of Bioprocess Engineering, Jiangxi Science & Technology Normal University, Nanchang 330013, People’s Republic © The Author(s) 2023. Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http:// creat iveco mmons. org/ licen ses/ by/4. 0/. Cui et al. Annals of Microbiology (2023) 73:3 Page 2 of 7 to test the affinity of acyl-CoA esters and over-expressed in Introduction M. ruber CICC41233 to measure Monascus pigment yield. Monascus pigment, belonging to natural edible pigments, The study of Mracbp2 gene could further reveal the is a red mold rice fermented by inoculating Monascus relationship between fatty acid synthesis and Monascus spp. with rice as a raw material. Monascus pigments have pigment synthesis. been widely used to brew rice wine and in fermented bean curd, vinegar, food coloring, meat products, Chinese medi- Materials and methods cine, etc. (Chen et al. 2015). Hajjaj et al. firstly reported Strains the Monascus pigment synthesis pathway involving fatty Monascus pigment production strain Monascus ruber acids and polyketide metabolism using isotope analysis CICC41233 was cultured on malt–peptone–starch (Hajjaj et al. 1999). The Monascus pigment biosynthesis in (MPS) agar. Escherichia coli DH5a was used to construct Monascus spp. was carried out using acyl-coenzyme A as a the vector. Escherichia coli BL21 was used to express the precursor through the polyketide pathway, which was cata- target protein. Agrobacterium tumefaciens EHA105 was lyzed by polyketide synthase (PKS) and fatty acid catalyzed used to transform the binary plasmid into M. ruber. by fatty acid synthase (FAS) (Hajjaj et al. 2000). In 2000, Hajjaj et al. reported that the effects of medium-chain fatty Construction of gene expression vectors acids on citrinin production and found that fatty acids, such The DNA and cDNA sequences of Mracbp2 gene as octanoic acid could increase the yield of Monascus pig- (MONRU_440654 of M. ruber NRRL1597 genome data- ment by 30 to 50% (Hajjaj et al. 2000). This result revealed base) were cloned from M. ruber CICC41233 using the association between fatty acid and Monascus pigment DNA and cDNA as the templates through polymerase synthesis. Recently, Monascus pigments biosynthesis gene chain reaction (PCR), using primers Mracbp2-F-PstIand cluster has been identified in Monascus purpureus (Bal - Mracbp2-R-KpnI, Mracbp2-F-EcoRI, and Mracbp2-R- akrishnan et al. 2013) and Monascus ruber M7 (Feng et al. Not, respectively (Supplementary Table S1). And then 2012; Chen et al. 2015), comprising the core elements, such the cloned gene sequences were sequenced by Beijing as PKS, FAS, dehydrogenase, transporter, regulator, etc. Genomics Institute (BGI) (China). Acyl-CoA binding protein (ACBP) is a highly con- Both DNA of the Mracbp2 gene fragment and the served protein found in all eukaryotic and prokaryotic binary expression vector pNeo0380 were digested with cells (Qiu and Zeng 2020). Two genes encoding ACBP are PstIand KpnI, respectively, and then ligated to construct found in filamentous fungi like Aspergillus oryzae (Kwon the vector pNeo0380-MrACBP2. et al. 2017). ACBP could bind with long-chain fatty acyl- Both cDNA of the Mracbp2 gene fragment and the CoA of different lengths with high specificity and high protein expression vector pGEX-6P-1 were digested with affinity and play multiple functions in the organism (Qiu EcoRIand NotI, respectively, and then ligated to construct and Zeng 2020). ACBP can mediate intracellular and the vector pGEX-MrACBP2. extracellular Acyl-CoA transport, maintain the stabil- ity of intracellular fatty Acyl-CoA library, protect it from Phylogenetic tree analysis hydrolysis, and participate in organelle biosynthesis, bio- The amino-acid sequence of Mr ACBP2 from M. ruber film assembly, and the regulation of lipid metabolism- CICC41233 was analyzed by Basic Local Alignment related genes and enzyme activities. Search Tool (BLAST) on the National Center for Bio- According to a previous study, MrACBP from Monas- technology Information (NCBI) (http:// www. ncbi. nlm. cus ruber CICC41233 has the highest binding affinity for nih. gov/ BLAST/) to obtain the homologous sequences. myristoyl-CoA. Monascus ruber ACBP5, the homolo- These sequences were aligned using CLUSTALX, and gously overexpressed Mracbp gene, showed the fatty acid then, a phylogenetic tree was constructed by MEGA 4 C14:0 decreased while the Monascus pigment increased software using the Neighbor-Joining method . (Long et al. 2018). In this study, a second acbp gene from M. ruber Protein expression and purification CICC41233, named Mracbp2, which was completely dif- The expression vector pGEX-MrACBP2 was transformed ferent from Mracbp was cloned. The keywords “acyl-coen - into E. coli BL21. One of the positive clones were selected zyme A binding protein” were used to search, and an acbp and activated overnight in 30-mL TB medium (contain- gene (transcript Id 440789) encoding ACBP protein (pro- ing 100 μg/mL ampicillin). Then, the 20-mL microbial tein ID 440654) was obtained from the Monascus ruber was transferred to 2 L TB medium (containing 100 μg/mL NRRL1597 genome database. Therefore, it was interesting ampicillin) and incubated at 37°C until OD =0.4~0.6. to identify the biochemical function of MrACBP2 in M. The isopropyl β-d-1-thiogalactopyranoside (IPTG) (final ruber. The gene Mracbp2 was expressed in Escherichia coli C ui et al. Annals of Microbiology (2023) 73:3 Page 3 of 7 concentration of 0.5 mM) was added as an inducer and fermentation medium (9.0% rice powder, 0.2% sodium incubated for 16 h at 16 °C. nitrate, 0.1% potassium dihydrogen phosphate, 0.2% mag- The bacteria were collected at 8000 rpm/min for 10 nesium sulfate heptahydrate, and 0.2% acetate, pH 3.2). min with 4°C. Later, 10 mL of GST binding buffer and Each strain was tested in triplicate, and the samples were 10 μL of PMSF (100 mM) were added, and the cells were taken 2 days and 6 days of fermentation (Long et al. 2018). resuspended by soaking, followed by centrifugation in an After fermentation, 25 mL of culture broth was centri- ice bath. Afterward, the supernatant was passed through fuged at 16 °C for 30 min at 9000 × g. The supernatant was a 0.45-μm microporous membrane filter to remove the the extracellular pigments (water-soluble pigment). The impurities and obtain the filtrate. The protein of interest precipitate was resuspended in 25 mL of 70% (v/v) ethanol was purified using the GST-tagged protein purification and incubated at 60 °C for 1 h with shaking at 90 × g and kit (BBI Life Sciences), and the eluted protein of interest then centrifuged at 16 °C for 15 min at 9000 × g. The super - was stored in a −80 °C refrigerator for further use. natant contained the intracellular pigment (ethanol-soluble The protein concentration was determined using a pigment). The residual mycelial precipitate was dried to a Bradford protein assay kit (Sangon Biotech Co. Ltd., constant weight at 60 °C to determine its biomass. Shanghai, China). The protein was denatured by incubat - The absorbance spectrum of the pigment sample was ing in boiling water for 10 min and directly analyzed by adjusted to 0.1–1.0 using a spectrophotometer at 510 sodium dodecyl sulfate-polyacrylamide gel electropho- nm. The result was expressed in the units of absorbance resis (SDS-PAGE) on a 10% polyacrylamide gel stained (U) at a given wavelength, multiplied by the dilution fac- with Coomassie brilliant blue. tor (Shi et al. 2015). The total MPs comprised water-sol - uble and ethanol-soluble pigments. Microscale thermophoresis binding analysis The microscale thermophoresis (MST) with a NanoTem - Transcription analysis per monolith NT.115 (CA, USA) was used to measure Transcription analysis was performed according to a pre- the binding ability of the recombinant protein pGEX- viously reported method (Long et al. 2018). The primers MrACBP2 for fatty acid acyl-CoA esters (from C4 to of gene GAPDH, pks, mppr1, fasA, and fasB are listed in C20). The recombinant protein was mixed with the gradi - Supplementary Table S1. ent-diluted ligand 1:1, and the light emitting diode (LED) power of microthermophoresis was 20% and the micro- Fatty acid content analysis scale thermophoresis power was 40%. The Kd value was The fatty acid analysis was conducted by GuangZhou Chem - analyzed by NanoTemper software (Jerabek-Willemsen ical Union Quality Testing Technology Co., Ltd (China). et al. 2011; Parker and Newstead 2014). Results and discussion Screening positive M. ruber transformants Cloning of Mracbp2 gene and phylogenetic tree analysis A. tumefaciens EHA105, containing a binary vector of MrACBP2 protein (pNeo0380-MrACBP2), was introduced into M. ruber The Mracbp2 was subjected to PCR to obtain the DNA CICC41233 through ATMT with G418 (80 μg/mL) as a fragments and cDNA fragments (Fig. 1) and sequenced screening marker (Balakrishnan et al. 2013). The transfor - by BGI. Subsequently, the DNA and cDNA fragments of mants were picked from the MPS agar (containing G418) 1525 bp and 1329 bp in length were obtained along with plate and then cultured thrice on MPS agar plates without three introns, respectively. This was different from the pre - G418. Single strains were transferred to MPS plates con- viously reported Mracbp gene from M. ruber CICC41233, taining G418 to determine the stability. The total genomic which has the DNA and cDNA of 629 bp and 450 bp in DNA was extracted from the mycelia following a previ- length, respectively, with two introns (Long et al. 2018). ously reported method by Balakrishnan et al. (2017). Posi- The deduced 442 amino-acid sequence of MrACBP2 tive transformants were identified by PCR amplification was aligned by BLAST on NCBI to obtain the homolo- using the primers PgpdA-OE-F and TtrpC-OE-R. gous sequences (Supplementary Sequence S1). These homologous sequences were used to construct a phyloge- Monascus pigment production analysis netic tree, as depicted in Fig. 2. The phylogenetic analysis After 7–10 days cultivation, the spores of M. ruber revealed that the MrACBP2 from M. ruber CICC41233 CICC41233 were obtained. The final concentration of was 100% confidence level to M. ruber NRRL1597. freshly harvested spores used for inoculation was 10 conidia/mL. The flasks were shaken at 30°C with a rota - Expression and purification of MrACBP2 protein tion speed of 180 rpm/min. The fermentation experi - In the TB broth without IPTG, MrACBP2 was not fully ment was carried out in a 250-mL flask, containing 50-mL expressed in E. coli BL21 (Fig. 3A, lane 1). However, Cui et al. Annals of Microbiology (2023) 73:3 Page 4 of 7 was consistent with the expected size by SDS-PAGE anal- ysis (Fig. 2B, lanes 1–4). The MrACBP2 exhibited binding preference for palmityl‑CoA The binding ability of the purified GST-ACBP2 fusion protein and acyl-CoA esters from C4 to C20 was detected by MST (Supplementary Fig. S1). As depicted in Fig. 4, the Kd value of GST-MrACBP2 for palmityl-CoA (C16- CoA) was 70.57 nM, which was the lowest value among of the all acyl-CoA esters. u Th s, the MrACBP2 clearly showed a binding preference for palmityl-CoA. The MrACBP2 from M.ruber CICC41233 was consist - ent with AoACBP of A. oryzae 3.042, exhibiting a binding preference for palmityl-CoA(Hao et al. 2016). However, Fig. 1 PCR amplification of Mracbp2 gene fragment from M.ruber it was different from the previously reported MrACBP CICC41233 (A Mracbp2 gene fragment from DNA. B Mracbp2 gene from M.ruber CICC41233, which exhibited a binding fragment from cDNA) preference for myristoyl-CoA (Long et al. 2018). with the addition of IPTG as an inducer, MrACBP2 was Comparison of Monascus pigment production between expressed more (Fig. 3A, lane 2). The predicted molecu - M.ruber CICC41233 and M.ruber ACBP2‑E lar weight of MrACBP2 was 51 kDa, and the molecular The pNeo0380-Mracbp2 vector was transformed into weight of GST-tag was 26 kDa. Thus, the purified fusion M.ruber CICC41233. A total of 11 transformants protein GST-ACBP2 was approximately 77 kDa, which were obtained and verified by PCR to be positive Fig. 2 Phylogeny analysis of MrACBP2 protein C ui et al. Annals of Microbiology (2023) 73:3 Page 5 of 7 Fig. 3 SDS-PAGE analysis of GST-MrACBP2 protein. (A Lane 1. No IPTG inducer; Lane 2. IPTG inducer; B Lanes 1–4. Purified target protein) Fig. 4 The affinity of Kd value between GST-MrACBP2 and fatty acyl-CoA analyzed by MST (error bars represent SD from duplicate replicates) transformants. After initial screening, one of the trans- formants which named M.ruber ACBP2-E was selected for subsequent experiments. As depicted in Fig. 5A, the pigment yield of M.ruber CICC41233 and M.ruber ACBP2-E increased with time. On the 6th day of fermentation, the yields of total pigment, ethanol-soluble pigment, and water-soluble Fig. 5 Monascus pigment production (A), biomass (B), and relative pigment increased by 63.61%, 71.61%, and 29.70%, expression fold (C) of M. ruber CICC41233, and M. ruber ACBP2-E respectively, M. ruber ACBP2-E compared with M.ruber CICC41233. The biomasses of the two strains after fermenta- unconventional secretion. The MrACBP2 from tion are depicted in Fig. 5B. The biomass of M.ruber M.ruber CICC41233 showed 56.0% homology with the ACBP2-E was always lower than that of M.ruber AoAcb2 protein. CICC41233 on 2 days (40.1%) and 6 days (27.9%), The expression levels of the genes are depicted in respectively. It was different from the Mracbp overex- Fig. 5C. The expression of Mracbp2 gene was increased pressed strain M.ruber ACBP5. There was no signifi- by 1.74-fold after a 2-day fermentation, and the expres- cant increase in the biomasses on 2 days and 4 days, sion of the pks, mppr1, fasA, and fasB genes increased but there was an increase in the biomasses on 6 days by 2.62-, 2.54-, 3.54-, and 4.92-fold, respectively. After (Long et al. 2018). Kwon et al. (2017) reported that 6 days of fermentation, the expression of Mracbp2 the Aoacb2 encoding acyl-CoA binding protein from gene was increased by 2.38-fold, and the expression A.oryzae is an essential gene for growth and undergoes Cui et al. Annals of Microbiology (2023) 73:3 Page 6 of 7 Table 1 Cellular fatty acid composition of M.ruber CICC41233 Strain M.ruber M.ruber ACBP2‑E M.ruber M.ruber ACBP2‑E CICC41233 48 h (%) CICC41233 144 h (%) Fatty acid 48 h (%) 144 h (%) C16:0 18.88±0.85 16.83±0.44* 19.36±0.06 15.22±0.46** C17:0 33.05±0.79 33.35±0.90 18.00±0.55 18.52±1.59 C18:0 4.84±0.15 4.86±0.07 11.98±0.02 11.30±0.41 C18:1 17.14±0.17 17.35±0.49 25.13±0.22 32.20±0.65** C18:2 26.09±0.20 27.60±0.10** 25.54±0.40 22.75±0.57** * ** p < 0.05, p < 0.01 of the pks, mppr1, fasA, and fasB genes decreased by Supplementary Information 63.7%, 76.2%, 76.1%, and 80.4%, respectively. The online version contains supplementary material available at https:// doi. org/ 10. 1186/ s13213- 023- 01710-1. Additional file 1 The following supporting information can be down- Fatty acid content analysis loaded at: ***Figure S1. The Kd values for ligand to bind of GST-MrACBP2 The contents of four fatty acids, including palmitic by MST. Table S1. Primers used in this study for polymerase chain reac- tion. Sequence S1. The sequences were used for phylogenetic analysis acid (C16:0), stearic acid (C18:0), oleic acid (C18:1), of ACBP2. and linoleic acid (C18:2), were measured and summa- rized in Table 1. The palmitic acid content in M.ruber Authors’ contributions ACBP2-E was significantly lower than that in M.ruber Jingjing Cui and Mengmeng Liu performed the experiments, analyzed the CICC41233 at 48 h and 144 h. This phenomenon was data, and wrote the manuscripts. Weiwei Wu performed the validation data. Chuannan Long modified the paper. Chuannan Long and Bin Zeng conceived, consistent with the previous study results. The fatty designed the experiments, and provided financial support. The authors read acid C14:0 content in M. ruber ACBP5 was lower than and approved the final manuscript. that in the M. ruber CICC41233 (Long et al. 2018). Funding This indicated that MrACBP2 was responsible for the This work was funded by the National Natural Science Foundation of China transport of intracellular acyl-CoA and the formation (grant no.31860436), Natural Science Foundation of Jiangxi Province (grant of an acyl-CoA ester pool (Knudsen et al. 1994; Færge- nos. 20181BAB204001, 20212BAB205002), Science and technology research project of Jiangxi Provincial Education Department (grant nos. GJJ211104, man et al. 2004; Xiao and Chye 2011; Yao et al. 2016). GJJ211118), Youth top-notch talent project of Jiangxi Science and Technology This was consistent with the strong binding selectivity Normal University (grant no. 2018QNBJRC004). of MrACBP2 to long-chain acyl-CoA, especially palmi- Availability of data and materials tyl-CoA, as shown by MST analysis. The datasets used and/or analyzed during the current study are available from There were no significant differences in stearic acid the corresponding author on reasonable request. content at 48 h and 144 h, and oleic acid content at 48h between M.ruber CICC41233 and M.ruber ACBP2-E. Declarations However, there were significant differences in linoleic Ethics approval and consent to participate acid content at 48 h and 144 h, and oleic acid content The study did not violate ethics, and all participants agreed to publish the at 144h between M.ruber CICC41233 and M.ruber paper. ACBP2-E. Consent for publication Not applicable. Conclusions In this study, a second acbp gene named as Mracbp2 from Competing interests The authors declare that they have no competing interests. M. ruber CICC41233 was cloned and showed the puri- fied fusion protein GST-Mr ACBP2 exhibited the high- est affinity for palmitoyl-CoA. Compared with M.ruber Received: 2 September 2022 Accepted: 30 December 2022 CICC41233, the palmitic acid content decreased, but the total Monascus pigments increased in the Mracbp2 gene overexpressed strain of M.ruber ACBP2-E. The results showed a significant difference between Mracbp and References Balakrishnan BJ, Karki S, Chiu SH, Kim HJ, Suh JW, Nam B, Yoon YM, Chen CC, Mracbp2 on the affinity of fatty acid for acyl-CoA esters. Kwon HJ (2013) Genetic localization and in vivo characterization of a However, these two genes could adjust the fatty acid syn- Monascus azaphilone pigment biosynthetic gene cluster. Appl Microbiol thesis and Monascus pigment syntheses. Biotechnol 97:6337–6345 C ui et al. Annals of Microbiology (2023) 73:3 Page 7 of 7 Balakrishnan B, Park SH, Kwon HJ (2017) A reductase gene mppE controls yellow component production in azaphilone polyketide pathway of Monascus. Biotechnol Lett 39(1):163–169 Chen WP, He Y, Zhou YX, Shao YC, Feng YL, Li M, Chen FS (2015) Edible filamen- tous fungi from the species Monascus: early traditional fermentations, modern molecular biology, and future genomics. Compr Rev Food Sci Food Saf 14:555–567 Færgeman NJ, Feddersen S, Christiansen JK, Larsen MK, Schneiter R, Unger- mann C, Mutenda K, RoepstorffP KJ (2004) Acyl-CoA-binding protein, Acb1p, is required for normal vacuole function and ceramide synthesis in Saccharomyces cerevisiae. Biochem J 380:907–918 Feng Y, Shao Y, Chen F (2012) Monascus pigments. Appl Microbiol Biotechnol 96(6):1421–1440 Hajjaj HA, Klaebe A, Loret MO, Goma G, Blanc PJ, Francois J (1999) Biosyn- thetic pathway of citrinin in the filamentous fungus Monascus ruber as revealed by 13C nuclear magnetic resonance[J ]. Appl Environ Microbiol 65(1):311–314 Hajjaj H, Klaébé A, Goma G, Blanc PJ, Barbier E, François J (2000) Medium-chain fatty acids affect citrinin production in the filamentous fungus Monascus ruber. Appl Environ Microbiol 66:1120–1125 Hao Q, Liu X, Zhao G, Jiang L, Li M, Zeng B (2016) Recombinant expression, purification, and characterization of an acyl-CoA binding protein from Aspergillus oryzae. Biotechnol Lett 38(3):519–525 Jerabek-Willemsen M, Wienken CJ, Braun D, Baaske P, Duhr S (2011) Molecular interaction studies using microscale thermophoresis. Assay Drug Dev Techn 9:342–353 Knudsen J, Faergeman NJ, Skøtt H, Hummel R, Børsting C, Rose TM, Andersen JS, Højrup P, Roepstorff P, Kristiansen K (1994) Yeast acyl-CoA-binding protein: acyl-CoA-binding affinity and effect on intracellular acyl-CoA pool size. Biochem J 302(2):479–485 Kwon HS, Kawaguchi K, Kikuma T, Takegawa K, Kitamoto K, Higuchi Y (2017) Analysis of an acyl-CoA binding protein in Aspergillus oryzae that undergoes unconventional secretion. Biochem Biophys Res Commun 493:481–486 Long C, Liu M, Chen X, Wang X, Ai M, Cui J, Zeng B (2018) The acyl-CoA bind- ing protein affects monascus pigment production in Monascus ruber CICC41233. 3 Biotech 8:121 Parker JL, Newstead S (2014) Molecular basis of nitrate uptake by the plant nitrate transporter NRT1.1. Nature 507:68–72 Qiu SK, Zeng B (2020) Advances in understanding the acyl-CoA-binding pro- tein in plants, mammals, yeast, and filamentous fungi. J Fungi 6:34 Shi K, Song D, Chen G, Pistolozzi M, Wu Z, Quan L (2015) Controlling composi- tion and color characteristics of Monascus pigments by pH and nitrogen sources in submerged fermentation. J Biosci Bioeng 120:145–154 Xiao S, Chye ML (2011) New roles for acyl-CoA-binding proteins (ACBPs) in plant development, stress responses and lipid metabolism. Prog Lipid Res 50:141–151 Yao YP, Ouyang CS, Jiang L, Liu XG, Hao Q, Zhao GZ, Zeng B (2016) Specificity of acyl-CoA binding protein to acyl-CoAs: influence on the lipid metabo - lism in Aspergillus oryzae. RSC Adv 6:94859–99486 Publisher’s Note Springer Nature remains neutral with regard to jurisdictional claims in pub- lished maps and institutional affiliations. Re Read ady y to to submit y submit your our re researc search h ? Choose BMC and benefit fr ? Choose BMC and benefit from om: : fast, convenient online submission thorough peer review by experienced researchers in your ﬁeld rapid publication on acceptance support for research data, including large and complex data types • gold Open Access which fosters wider collaboration and increased citations maximum visibility for your research: over 100M website views per year At BMC, research is always in progress. Learn more biomedcentral.com/submissions
Annals of Microbiology – Springer Journals
Published: Jan 7, 2023
Keywords: Acyl-CoA binding protein; M. ruber CICC41233; Mracbp2 gene; Affinity; Monascus pigments
Access the full text.
Sign up today, get DeepDyve free for 14 days.