The genus Macaranga belongs to the family Euphorbiaceaeconsistingof about 300 species that are mainly distributed inthe tropics of Africa, Asia, Australia, and the Pacific regions. Thirteen different species of this genus occur in Viet Nam, and Macaranga sampsonii has been used in traditional medicine to treat swellings, cuts, sores. Phytochemical investigation of the methanol extract of Macaranga sampsonii led to the isolation of six compounds including: boehmenan X (1), maltol β‐D‐glucopyranoside (2), methyl brevifolincarboxylate (3), scopoletin (4), 3,5‐dihydroxy‐4‐methoxy benzoic acid (5) and gallic acid (6). Their structures were confirmed by spectroscopic methods including IR, MS, 1D, 2D NMR and compared to previous reported spectral data values.

Cardiovascular disease is the leading cause of death in the world. Cardiovascular risk assessment is an important step in preventing and treating the disease. The current study assesses the 10-year risk of cardiovascular disease in 306 VNU’s office workers in 2016-2017 based on the 2008 Framingham Risk Score. The study results show that the average risk score was 4.05 ± 4.76%; low risk was 90.52%; moderate risk: 7.85 %; and high to very high risk was 1.63%. Men have a higher risk score than women (p <0.001). The ten-year cardiovascular risk score shows that age and systolic blood pressure correlated with the risk at a medium level, and cholesterol and HDL correlated with it at a low level. Keywords Framingham Risk Score 2008, 10-year cardiovascular risk score, hypertension, blood cholesterol, blood HDL. References [1] Cardiovasculardiseases, http://www.who.int/en/newsroom/factsheets/detail/cardiovascular diseases-(cvds), (truy cập ngày 22/03/2019).[2] A.R. Gregory et al, Global, regional, and national burden of cardiovascular diseases for 10 Causes, 1990 to 2015, Journal of the American college of cardiology. 70(1) (2017) 1–25.[3] E. Gresham, T.E. Fitzpatrick, P.A. Wolf et al, Residual disability in survivors of stroke--the Framingham study, N Engl J Med. 293(19) (1975) 954–956.[4] T.A. Pearson, S.N. Blair, S.R. Danielset et al, AHA guidelines for primary prevention of cardiovascular disease and stroke: 2002 update: consensus panel guide to comprehensive risk reduction for adult patients without coronary or other atherosclerotic vascular diseases, American heart association science advisory and coordinating committee, Circulation. 106(3) (2002) 388–391.[5] I. Graham, D. Atar, K. B. Johnsen et al, European guidelines on cardiovascular disease prevention in clinical practice: full text - Fourth joint task force of the European society of cardiology and other societies on cardiovascular disease prevention in clinical practice constituted by representatives of nine societies and by invited experts, Euro heart J. 28(19) (2007) 2375-2414.[6] S.S. Mahmood, D. Levy, R.S. Vasanet et al, The Framingham heart study and the epidemiology of cardiovascular diseases: a historical perspective, Lancet. 383(9921) (2014) 999–1008.[7] J.A.A.G. Damen, L. Hooft, E. Schuit et al, Prediction models for cardiovascular disease risk in the general population: systematic review, BMJ. 353(2016) 1-10.[8] L.Q.H. Goh, T.A. Welborn, S.S. Dhaliwal, Independent external validation of cardiovascular disease mortality in women utilising Framingham and SCORE risk models: a mortality follow-up study, BMC women health. 14 (2014) 118-129.[9] L.M. A. Rodenas, J.A. C. Herencia, J.A. D. Garrote et al, Framingham risk score for prediction of cardiovascular diseases: a population-based study from southern Europe, PLoS One. 8(9) (2013) 1-10.[10] G.M. Park, Y.H. Kim, Model for predicting cardiovascular disease: insights from a Korean cardiovascular risk model, Pulse (Basel). 3(2) (2015) 153–157.[11] Trần Kim Trang, Nguy cơ 10 năm của bệnh tim mạch ở nữ giới tăng huyết áp, Y học thành phố Hồ Chí Minh. 16(1) (2012) 181-185.[12] Trương Thanh Sơn, Nguyễn Văn Trí, Trương Quang Bình, Nghiên cứu áp dụng thang điểm Framingham nhằm định nguy cơ bệnh động mạch vành trong 10 năm tới tại bệnh viện đa khóa Bình Dương, Y học thành phố Hồ Chí Minh. 15(1) (2011) 207-212. [13] Nguyễn Thị Kim Thủy, Dự báo nguy cơ mắc bệnh động mạch vành trong 10 năm theo thang điểm Frammingham ở bệnh nhân tăng huyết áp nguyên phát, Y học thực hành. 802(1) (2012) 27-29. [14] Nguyễn Hồng Huệ, Nguyễn Đức Công, Nghiên cứu ước tính nguy cơ bệnh động mạch vành trong 10 năm tới theo thang điểm Framingham qua 500 trường hợp, Y học thành phố Hồ Chí Minh. 15(2) (2011) 38-44. [15] C.V. Aram et al, The seventh report of the joint national committee on prevention, detection, evaluation, and treatment of high blood pressure, National heart, lung and blood institute - National institutes of health, NIH publication no. 04-5230, US, (2014), pp 13.[16] National Heart, Lung and Blood Institute, Third Report of the national cholesterol education program (NCEP) expert panel on detection, evaluation, and treatment of high blood cholesterol in adults (Adult treatment panel III) Final report, National institutes of health, part II, US, (2002), pp 5-10. [17] World Health Organization, The Asia-Pacific perspective: redefining obesity and its treatment, Geneva: World health organization western pacific regional office, (2000), 18-19.[18] N.Q. Nguyen, S.T. Pham, L.D. Do et al, Cardiovascular disease risk factor patterns and their implications for intervention strategies in Vietnam, Int J Hypertens, ID. 560397, (2012), 1-11.[19] M. Nakhaie, B. Koor, S. Salehiet al, Prediction of cardiovascular disease risk using framingham risk score among office workers, Iran, 2017, Saudi journal of kidney diseases and transplantation. 29(3) (2018) 608-614. [20] Trịnh Xuân Thắng, Nghiên cứu các yếu tố nguy cơ bệnh tim mạch ở người >25 tuổi tại 2 quận huyện Hà Nội, Luận văn thạc sỹ, Đại học Y Hà Nội, (2013). [21] Nguyễn Hoàng Liên, Văn Thế Trung, Xác định nguy cơ tim mạch theo thang điểm Framingham trên bệnh nhân vẩy nến tại bệnh viện da liễu TP. Hồ Chí Minh, Y Học TP. Hồ Chí Minh, 18(1), (2014), 79-85. [22] R. Gupta, V. Kaul, A. Agrawalet et al, Cardiovascular risk according to educational status in India, Preventive medicine. 51(5) (2010) 408–411.[23] C.A. Jones, L. Ross, N. Suraniet al, Framingham ten-year general cardiovascular disease risk: agreement between BMI-based and cholesterol-based estimates in a South Asian convenience sample, PLOS ONE. 10(3) (2015) e0119183.[24] K.S. Tyrrell, H.C. Lassila, E. Meilahn et al, Carotid atherosclerosis in premenopausal and postmenopausal women and its association with risk factors measured after menopause, Stroke. 29(6) (1998) 1116–1121.[25] Margaret Kelly Hayes et al, Influence of age and health behaviors on stroke risk: lessons from longitudinal studies, J Am Geriatr Soc. 58(2) (2010) 325–328.[26] D. Sugiyama, T. Okamura, M. Watanabe et al, Risk of hypercholesterolemia for cardiovascular disease and the population attributable fraction in a 24-year Japanese cohort study, J Atheroscler Thromb. 22(1) (2015) 95–107.[27] M.R. Law, N.J. Wald, S.G. Thompson, By how much and how quickly does reduction in serum cholesterol concentration lower risk of ischaemic heart disease, BMJ. 308(6925) (1994) 367–372.[28] Abolfazl Mohammadbeigi et al, Dyslipidemia prevalence in Iranian adult men: the impact of population-based screening on the detection of undiagnosed patients, World J men health. 33(3) (2015) 167-173. [29] R.S. Joshi et al, Prevalence of dyslipidemia in urban and rural India: The ICMR–INDIAB Study, PloS ONE. 9(5) (2014) 1-9.[30] Wichai Aekplakorn et al, Prevalence of dyslipidemia and management in the Thai population: national health examination survey IV, 2009, Journal of lipids. (2014) 1-13.[31] Asia Pacific, Cohort Studies Collaboration, cholesterol, diabetes and major cardiovascular diseases in the Asia-pacific region, Diabetologia. 50(11) (2003) 2289-2297.[32] S. Lewington, R. Clarke, N. Qizilbash, R. Peto, R. Collins et al, Age-specific relevance of usual blood pressure to vascular mortality: a meta-analysis of individual data for one million adults in 61 prospective studies, Lancet. 360(9349) (2002) 1903–1913.[33] Viet Nam national STEPS Survey 2015, https://www.who.int/ncds/un-task-force/steps-survey-vietnam2015.pdf, (2015), (truy cập ngày 09/03/2019).[34] Nguyễn Lân Việt, Kết quả mới nhất điều tra tăng huyết áp toàn quốc năm 2015 – 2016, Hội tim mạch Việt Nam, http://www.yhth.vn/hoinghitanghuyetapvietnamlanthuii_d3378.aspx, (2016) (truy cập ngày 11/02/2019).[35] M. Satoh, et al, Combined effect of blood pressure and total cholesterol levels on long-term risks of subtypes of cardiovascular death: evidence for cardiovascular prevention from observational cohorts in Japan, hypertension. 65(3) (2015) 517–524.

The incidence of type 2 diabetes mellitus is rapidly increasing, with many complications pressured on the health care system. Complications of diabetes due to chronic hyperglycemia related to other metabolic disorders, causing damage to the microvascular system. Among them, damaged kidney vessels lead to impair the renal function as diabetic nephropathy is the most common cause of end-stage renal disease. Measurement of glomerular filtration rate (GFR) is an important parameter in assessing renal function. In Vietnam’s hospital, serum creatinine is the biomarker mostly used to assess GFR. However, this biomarker is affected many factors such as gender, age, ... Many studies showed that serum Cystatin C is another biomarker that can detect early decline in GFR, less affected by other factors. Therefore, we conducted this study to explore serum cystatin C and creatinine levels in patients with type 2 diabetes and initially compare GFR in applying formulas of CKD.EPI 2012 and age and sex factors with these two biomarkers on those patient groups. The prospective, descriptive, cross-sectional study was performed on 50 patients with type 2 diabetes. Serum Cystatin C, serum creatinine test was performed and GFR was estimated by CKD.EPI 2012 equation. The results showed that the average serum Cystatin C level of the study group was 0.87 ± 0.24 mg/L that expressed no difference between two genders, and significant difference between age groups. Whereas, the average serum creatinine level of the study group was 81.30 ± 19.70 µmol/L, significant difference between male and female but not difference between age groups. In patients with GFR <60 mL/min/1.73m2, serum creatinine and cystatin C levels were higher than normal but there was no difference with the upper limit in the normal reference range of the two indications. Keyword Type 2 diabetes, serum cystatin C, serum creatinine, glomerular filtration rate. References [1] N.H. Cho, J. Kirigia, J.C. Mnanya, K. Ogurstova, L. Gủaiguata, W. Rathmann, G. Roglic, N. Forouhi, R. Dajani, A. Esteghmati, E. Boyko, L. Hambleton, O.L.M. Neto, P.A. Montoya, S. Joshi, J. Chan, J. Shaw, T.A. Samuels, M. Pavkov, A. Reja, IDF Diabetes Atlas eight edition, International Diabete Federation, 2017. http://fmdiabetes.org/wp-content/uploads/2018/03/IDF-2017.pdf (access 15 july 2019).[2] G. Xu, B. Liu, Y. Sun, Y. Du, L.G. Snetselaar, F.B. Hu, W. Bao, Prevalence of diagnosed type 1 and type 2 diabetes among US adults in 2016 and 2017: population based study, British Medical Journal 361 (2018) k1497. https://doi.org/ 10.1136/bmj.k1497.[3] N.T.T. Minh, N.K. Luong, N.K. Son, The clinical and subclinical characteristics in patients with diabetes mellitus treated at Thai Nguyen General hospital, Journal of pratical medicine 787 (2011) 25-8.[4] N.T.H. Lan, L.D. Tuan, Survey characteristics of renal complication in elderly type 2 diabetes outpatients treated at National Hospital of Endocrinology, Journal of Military Pharmaco-medicine 6 2017 55-62. [5] Mohsen Pourghasem, Hamid Shafi, Zahra, Histological changes of kidney in diabetic nephropathy, Caspian J Intern Med 6(3) (2015) 120-7. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4650785/pdf/cjim-6-120.pdf (access 16 july 2019).[6] D.W. Powell, D.N. Kenagy, S. Zheng, S.C. Coventry, J. Xu, L. Cai, E.C. Carlson, P.N. Epstein, Associations between Structural and Functional Changes to the Kidney in Diabetic Humans and Mice, Life Sci 93(7) (2013) 257-64. https://doi.org/ 10.1016/j.lfs.2013.06.016.[7] Natalie Ebert, Elke Schaeffner, New biomarkers for estimating glomerular filtration rate, Journal of Laboratory and Precision Medicine 3(75) (2018. https://doi.org/10.21037/jlpm.2018.08.07.[8] L.A. Inker, C.H. Schmid, H. Tighiouart, J.H. Eckfeldt, H.I. Feldman, T. Greene, J.W. Kusek, J. Manzi, F.V. Lente, Y.L. Zhang, J. Coresh, A.S. Levey, Estimating Glomerular Filtration Rate from Serum Creatinine and Cystatin C, The new England Journal of Medicine 367 (2012) 20-9. https://doi.org/ 10.1056/NEJMoa1114248.[9] Ashwin Kumar, Anil Kumar, Serum cystatin C and serum creatinine levels in type 2 diabetes mellitus, International Journal of Research in Medical Sciences 3(1) (2015) 174-7. https://doi.org/10.5455/2320-6012.ijrms20150130.[10] X. Jianguo, D.I. Broadhurst, M. Wilson, D.S. Wishart, Translational biomarker discovery in clinical metabolomics:an introductory tutorial, Metabolomics 9 (2013) 280–99. https://doi.org/ 10.1007/s11306-012-0482-9.[11] B.T. Anh, Estimate the glomerular filtration rate by plasma creatinine and cystatin C concentration, Journal of Vietnam Medicine 2 (2012) 12-18.[12] S. Kakde, S. Alexander, V.G. David, S. Jacob, A. Mohapatra, A.T. Valson, B. Gopal, C.K. Jacob, J. Hephzibah, V. Tamilarasi, S. Varughese, Relationship of creatinine and cystatin C-based estimated glomerular filtration rates with measured glomerular filtration rate in healthy kidney donors from South Asia, Indian J Nephrol 28 (2018) 345-50. https://doi.org/ 0.4103/ijn.IJN 249_17[13] Olympus life science research europa GmbH, Olympus clinical chemistry reagent guide, Olympus Diagnostic, American, 2009.[14] International Society of Nephrology, KDIGO 2012 clinical practice guideline for the evaluation and Management of chronic kidney disease, Kidney Int, Kidney International Supplements 3(1) (2012) 5-14. https://kdigo.org/wp-content/uploads/2017/02/KDIGO_2012_CKD_GL.pdf (access 19 july 2019).[15] American Diabete Association, Classification and Diagnosis of Diabetes: Standards of Medical Care in Diabetes 2018. Diabetes Care, (41(Supplement 1)) (2018) S13-S27. https://diabetesed.net/wp-content/uploads/2017/12/2018-ADA-Standards-of-Care.pdf (access 18 july 2019).[16] L.S. Weinert, A.B. Prates, F.B. do Amaral, M.Z. Vaccoro, J.L. Camargo, S.P. Silveiro, Gender does not influence cystatin C concentrations in healthy volunteers, Clin Chem Lab Med 48(3) (2010) 405-8. https://doi.org/10.1515/CCLM.2010.068.[17] N.T. Ly, T.T.C. Mai, Serum cystatin C and renal function in type 2 diabetic patients, Journal of medical Research 80(3B) (2012) 17-O.Al.[18] Musaimia, A.H. Abu-Nawwas, D.Al. Shaera, N.Y.Khaleela, M.Fawzi, Influence of age, gender, smoking, diabetes, thyroid and cardiac dysfunctions on cystatin C biomarker, Medicina de Familia Semergen 45(1) (2019) 44-51. https://doi.org/ 10.1016/j.semerg.2018.07.005.[19] M.C. Odden, I.B. Tager, R.T. Gansevoort, S.J.L. Bakker, R. Katz, L.F. Fried, et al, Age and cystatin C in healthy adults: a collaborative study, Nephrol Dial Transplant 25(2) (2010) 463-9. https://doi.org/10.1093/ndt/gfp474.[20] E.D. O’ Sullivan, J. Hughes, D.A. Ferenbach, Renal Aging: Causes and Consequences, J Am Soc Nephrol 28 (2017) 407–20. https://doi.org/10.1681/ASN.2015121308.[21] E.D. O’ Sullivan, J. Hughes, D.A. Ferenbach, Renal Aging: Causes and Consequences, J Am Soc Nephrol 28 (2017) 407–20. https://doi.org/10.1681/ASN.2015121308.[22] Christiane Oddoze, Henri Portugal, Yvon Berland, Bertrand Dussol, Cystatin C Is Not More Sensitive Than Creatinine for Detecting Early Renal Impairment in Patients With Diabetes. American Journal of Kidney Diseases, 38(2 (August)), (2001) 310-6. https://doi.org/ 10.1053/ajkd.2001.26096.    

Diabetes Mellitus has been becoming a disease of the century, and disease incidence is still rising worldwide. It causes many serious complications, especially in the eye, heart, kidneys, brain, and vascular system, such as diabetic nephropathy, diabetic retinopathy, liver fa­ilure, etc. Moreover, the process of controlling this disease is complicated. Meanwhile, the antidiabetic drugs on the market are facing some problems with a wide range of adverse reactions. Therefore, finding new drugs to treat diabetes has always been a topic that many researchers are interested in, especially drugs derived from nature like microorganisms and medicinal plants. This review is to provide knowledge concerning the effects of α-glucosidase inhibitors, which are oral antidiabetic drugs commonly used for diabetes mellitus type 2. Besides, we show readers the variety of active ingredients originating from nature, particularly the secondary metabolites of Aspergillus spp., which have many applications in the chemical and medicinal industry. Keywords: Diabetes, α-glucosidase inhibitors, Aspergillus. References [1] W. H. Organization, Classification of Diabetes Mellitus, https://www.who.int/westernpacific/health-topics/diabetes (accessed on: May 11th, 2021).[2] J. Thrasher, Pharmacologic Management of Type 2 Diabetes Mellitus: Available Therapies, Am J Cardiol, Vol. 120, No. 1, 2017, pp. S4-S16, https://doi.org/10.1016/j.amjcard.2017.05.009.[3] W. Hakamata, M. Kurihara, H. Okuda, T. Nishio, T. Oku, Design and Screening Strategies for Alpha-glucosidase Inhibitors Based on Enzymological Information, Curr Top Med Chem, Vol. 9, No. 1, 2009, pp. 3-12, https://doi.org/10.2174/156802609787354306.[4] US, Patent Version Number: US4062950A, Amino Sugar Derivatives, https://patents.google.com/patent/US4062950A/en(accessed on: May 11th, 2021).[5] A. S. Dabhi, N. R. Bhatt, M. J. Shah, Voglibose: an Alpha- glucosidase Inhibitor, J Clin Diagn Res, Vol. 7, No. 12, 2013, pp. 3023-3027, https://doi.org/10.7860/JCDR/2013/6373.3838.[6] P. Durruty, M. Sanzana, L. Sanhueza, Pathogenesis of Type 2 Diabetes Mellitus, Type 2 Diabetes - from Pathophysiology to Modern Management, Intechopen, United Kingdom, 2019, pp. 1-18.[7] L. N. Khue, T. H. Dang, T. H. Quang, N. T. Khue et al., Guidelines for Diagnosis and Treatment of Diabetes Type 2, Ministry of Health, Vietnam, 2021 (in Vietnamese).[8] M. Okuyama, W. Saburi, H. Mori, A. Kimura, Alpha-Glucosidases and Alpha-1,4-Glucan Lyases: Structures, Functions, and Physiological Actions, Cell Mol Life Sci, Vol. 73, 2016, pp. 2727-2751, https://doi.org/10.1007/s00018-016-2247-5.[9] V. L. Yip, S. G. Withers, Nature's Many Mechanisms for The Degradation of Oligosaccharides, Org Biomol Chem, Vol. 19, No. 2, 2004, pp. 2707-2713, https://doi.org/10.1039/B408880H.[10] B. Henrissat, A. Bairoch, New Families in The Classification of Glycosyl Hydrolases Based on Amino Acid Sequence Similarities, Biochem J, Vol. 293, No. 3, 1993, pp. 781-788, https://doi.org/10.1042/bj2930781.[11] B. Henrissat, A Classification of Glycosyl Hydrolases Based on Amino Acid Sequence Similarities, Biochem J, Vol. 280, No. 2, 1991, pp. 309-316, https://doi.org/10.1042/bj2800309.[12] R. Gupta, P. Gigras, H. Mohapatra, V. K. Goswami, B. Chauhan, Microbial A-amylases: A Biotechnological Perspective, Process Biochemistry, Vol. 38, No. 11, 2003, pp. 1599-1616, https://doi.org/10.1016/s0032-9592(03)00053-0.[13] C. V. D. Maarel, B. V. D. Veen, J. C .M. Uitdehaag, H. Leemhuis, L. Dijkhuizen, Properties and Applications of Starch-Converting Enzymes of The A-Amylase Family, Journal of Biotechnology, Vol. 94, No. 2, 2002, pp. 137-155, https://doi.org/10.1016/s0168-1656(01)00407-2.[14] N. R. Kim, D. W. Jeong, D. S. Ko, J. H. Shim, Characterization of Novel Thermophilic Alpha-Glucosidase from Bifidobacterium Longum, Int J Biol Macromol, Vol. 99, 2017, pp. 594-599, https://doi.org/10.1016/j.ijbiomac.2017.03.009.[15] D. R. Rose, M. M. Chaudet, K. Jones, Structural Studies of The Intestinal Alpha-Glucosidases, Maltase-glucoamylase and Sucrase-isomaltase, J Pediatr Gastroenterol Nutr, Vol. 66, No. 3, 2018, pp. S11-S13, https://doi.org/10.1097/MPG.0000000000001953.[16] L. Ren, X. Qin, X. Cao, L. Wang, F. Bai, G. Bai, Y. Shen, Structural Insight into Substrate Specificity of Human Intestinal Maltase-Glucoamylase, Protein Cell, Vol. 2, 2011, pp. 827-836, https://doi.org/10.1007/s13238-011-1105-3.[17] L. Sim, C. Willemsma, S. Mohan, H. Y. Naim, B. M. Pinto, D. R. Rose, Structural Basis for Substrate Selectivity in Human Maltase-Glucoamylase and Sucrase-Isomaltase N-Terminal Domains, J Biol Chem, Vol. 285, No. 23, 2010, pp. 17763-17770, https://doi.org/10.1074/jbc.M109.078980.[18] K. Jones, L. Sim, S. Mohan, J. Kumarasamy,H. Liu, S. Avery, H. Y. Naim, R. Q. Calvillo, B. L. Nichols, B. M. Pinto, D. R. Rose, Mapping The Intestinal Alpha-Glucogenic Enzyme Specificities of Starch Digesting Mal se-Glucoamylase and Sucrase-Isomaltase, Bioorg Med Chem, Vol. 19, 2011, pp. 3929-3934, https://doi.org/10.1016/j.bmc.2011.05.033.[19] P. T. T. Chau, P. T. Nghia, Enzyme and Application, Education Publisher, Vietnam, 2009.[20] Researchgate, Food Protein-Derived Bioactive Peptides in Management of Type 2 Diabetes - Scientific Figure, https://www.researchgate.net/figure/Mechanism-of-action-of-alpha-glucosidase-inhibitors_fig2_279991207 (accessed on: May 10th, 2021).[21] Z. Liu, S. Ma, Recent Advances in Synthetic Alpha-Glucosidase Inhibitors, Chem Med Chem, Vol. 12, No. 11, 2017, pp. 819-829, https://doi.org/10.1002/cmdc.201700216.[22] A. Lee, P. Patrick, J. Wishart, M. Horowitz, J. E. Morley, The Effects of Miglitol on Glucagon-Like Peptide-1 Secretion And Appetite Sensations in Obese Type 2 Diabetics, Diabetes Obes Metab, Vol. 4, No. 5, 2002, pp. 329-335, https://doi.org/10.1046/j.14631326.2002.00219.x.[23] I. Takei, K. Miyamoto, O. Funae, N. Ohashi, S. Meguro, M. Tokui, T. Saruta, Secretion of GIP in Responders to Acarbose in Obese Type 2 (NIDDM) Patients, Journal of Diabetes and Its Complications, Vol. 15, No. 5, 2001, pp. 245-249, https://doi.org/10.1016/s1056-8727(01)00148-9.[24] X. Bian, X. Fan, C. Ke, Y. Luan, G. Zhao, A. Zeng, Synthesis and Alpha-Glucosidase Inhibitory Activity Evaluation of N-Substituted Aminomethyl-Beta-D-Glucopyranosides, Bioorg Med Chem, Vol. 21, No. 17, 2013, pp. 5442-5450, https://doi.org/10.1016/j.bmc.2013.06.002.[25] J. B. Yang, J. Y. Tian, Z. Dai, F. Ye, S. C. Ma, A. G. Wang, α-Glucosidase Inhibitors Extracted from The Roots of Polygonum Multiflorum Thunb, Fitoterapia, Vol. 117, 2017, pp. 65-70, https://doi.org/10.1016/j.fitote.2016.11.009.[26] Z. Yin, W. Zhang, F. Feng, Y. Zhang, W. Kang, α-Glucosidase Inhibitors Isolated from Medicinal Plants, Food Science and Human Wellness, Vol. 3, No.3-4, 2014, pp. 136-174, https://doi.org/10.1016/j.fshw.2014.11.003.[27] P. Qiu, Z. Liu, Y. Chen, R. Cai, G. Chen, Z. She, Secondary Metabolites with Alpha-Glucosidase Inhibitory Activity from The Mangrove Fungus Mycosphaerella sp. SYSU-DZG01, Mar Drugs, Vol. 17, No. 8, 2019, pp. 483-508, https://doi.org/10.3390/md17080483.[28] S. Munasaroh, S. R. Tamat, R. T. Dewi, Isolation and Identification of α-Glucosidase Inhibitor from Aspergillus Terreus F38, Indonesian Journal of Pharmacy, Vol. 29, No. 2, 2018, pp. 74-79, https://doi.org/10.14499/indonesianjpharm29iss2pp74.[29] R. T. Dewi, A. Suparman, H. Mulyani, P. D. N. Lotulung, Identification of A New Compound as α-Glucosidase Inhibitor from Aspergillus Aculeatus, Annales Bogorienses, Vol. 20, No. 1, 2016, pp. 19-23, https://doi.org/10.14203/ann. bogor .2016.v20.n1.19-23.[30] R. T. Dewi, S. Tachibana, A. Darmawan, Effect on α-Glucosidase Inhibition and Antioxidant Activities of Butyrolactone Derivatives from Aspergillus Terreus MC751, Medicinal Chemistry Research, Vol. 23, 2014, pp. 454-460, https://doi.org/10.1007/s00044-013-0659-4.[31] M. G. Kang, S. H. Yi, J. S. Lee, Production and Characterization of A New Alpha-Glucosidase Inhibitory Peptide from Aspergillus Oryzae N159-1, Mycobiology, Vol. 41, No. 3, 2013, pp. 149-154, https://doi.org/10.5941/MYCO.2013.41.3.149.[32] S. Onose, R. Ikeda, K. Nakagawa, T. Kimura, K. Yamagishi, O. Higuchi, T. Miyazawa, Production of The Alpha-Glycosidase Inhibitor 1-Deoxynojirimycin from Bacillus Species, Food Chem, Vol. 138, No. 1, 2013, pp. 516-523, https://doi.org/10.1016/j.foodchem.2012.11.012.[33] Y. P. Zhu, K. Yamaki, T. Yoshihashi, M. Ohnishi Kameyama, X. T. Li, Y. Q. Cheng, Y. Mori, L. T. Li, Purification and Identification of 1-Deoxynojirimycin (DNJ) in Okara Fermented by Bacillus Subtilis B2 from Chinese Traditional Food (Meitaoza), J Agric Food Chem, Vol. 58,No. 7, 2010, pp. 4097-4103, https://doi.org/10.1021/jf9032377.[34] A. Tabussum, N. Riaz, M. Saleem, M. Ashraf, M. Ahmad, U. Alam, B. Jabeen, A. Malik, A. Jabbar, α-Glucosidase Inhibitory Constituents from Chrozophora Plicata, Phytochemistry Letters, Vol. 6, No. 4. 2013, pp. 614-619, https://doi.org/10.1016/j.phytol.2013.08.005.[35] M. Yagi, T. Kouno, Y. Aoyagi, H. Murai, The Structure of Moranoline, A Piperidine Alkaloid from Morus Species, Journal of The Agricultural Chemical Society of Japan, Vol. 50, No. 11, 1976, pp. 571-572, https://doi.org/10.1271/nogeikagaku1924.50.11_571.[36] M. Hemker, A. Stratmann, K. Goeke, W. Schroder, J. Lenz, W. Piepersberg, H. Pape, Identification, Cloning, Expression, and Characterization of The Extracellular Acarbose-Modifying Glycosyltransferase, AcbD, from Actinoplanes Sp. Strain SE50, J Bacteriol, Vol. 183, No. 15, 2001, pp. 4484-4492, https://doi.org/10.1128/JB.183. 15.4484-4492.2001.[37] E. Truscheit, I. Hillebrand, B. Junge, L. Müller, W. Puls, D. Schmidt, Microbial α-Glucosidase Inhibitors: Chemistry, Biochemistry, and Therapeutic Potential, Presented at Drug Concentration Monitoring Microbial alpha-Glucosidase Inhibitors Plasminogen Activators, Springer-Verlag, Berlin, 1988.[38] Y. Kameda, N. Asano, M. Yoshikawa, M. Takeuchi, T. Yamaguchi, K. Matsui, S. Horii, H. Fukase, Valiolamine, A New Alpha-Glucosidase Inhibiting Aminocyclitol Produced by Streptomyces Hygroscopicus, J Antibiot (Tokyo), Vol. 37, No. 11, 1984, pp. 1301-1307, https://doi.org/10.7164/antibiotics.37.1301.[39] D. T. Tuyen, V. V. Hanh, V. T. T. Hang, D. K. Trinh, D. T. Quyen, Extraction and Purification of DNJ (1-Deoxynojirimycin) Inhibiting α-Glucosidase from B. Subtilis VN9 Strain Isolated from Vietnam, National Biotechnology Conference, 2013.[40] D. T. Tuyen, Optimization and Purification of α-Glucosidase Inhibitor from Bacillus Subtilis YT20 Isolated in Vietnam, Vietnam Journal of Science and Technology, Vol. 59, No. 2, 2021, pp. 179-188, https://doi.org/10.15625/2525-2518/ 59/2/14928.[41] S. E. Baker, J. W. Bennett, An Overview of the Genus Aspergillus, Aspergillus: Molecular Biology and Genomics, The Aspergilli, Taylor & Francis, United Kingdom, 2008, pp. 3-13.[42] H. C. Gugnani, Ecology and Taxonomy of Pathogenic Aspergilli, Front Biosci, Vol. 8, No. 6, 2003, pp. s346- s357, https://doi.org/10.2741/1002.[43] C. G. Shaw, The Genus Aspergillus, Science, Vol. 150, No. 3697, 1965, pp. 736-737, https://doi.org/10.1126/science.150.3697.736-a.[44] M. T. Hedayati, A. C. Pasqualotto, P. A. Warn, P. Bowyer, D. W. Denning, Aspergillus Flavus: Human Pathogen, Allergen and Mycotoxin Producer, Microbiology, Vol. 153, No. 6, 2007, pp. 1677-1692, https://doi.org/10.1099/mic.0.2007/007641-0.[45] T. R. Dagenais, N. P. Keller, Pathogenesis of Aspergillus Fumigatus in Invasive Aspergillosis, Clin Microbiol Rev, Vol. 22, No. 3, 2009, pp. 447-465, https://doi.org/10.1128/CMR.00055-08.[46] S. Amaike, N. P. Keller, Aspergillus Flavus, Annu Rev Phytopathol, Vol. 49, 2011, pp. 107-133, https://doi.org/10.1146/annurev-phyto-072910-095221.[47] J. Houbraken, R. P. De Vries, R. A. Samson, Modern Taxonomy of Biotechnologically Important Aspergillus and Penicillium Species, Adv Appl Microbiol, Vol. 86, 2014, pp. 199-249, https://doi.org/10.1016/B978-0-12-800262-9.00004-4.[48] E. Ichishima, Development of Enzyme Technology for Aspergillus Oryzae, A. Sojae, and A. Luchuensis, The National Microorganisms of Japan, Biosci Biotechnol Biochem, Vol. 80, No. 9, 2016, pp. 1681-1692, https://doi.org/10.1080/09168451.2016.1177445.[49] E. Schuster, N. Dunn-Coleman, J. C. Frisvad, P. W. Van Dijck, on The Safety of Aspergillus Niger-A Review, Appl Microbiol Biotechnol, Vol. 59, No. 4-5, 2002, pp. 426-435, https://doi.org/10.1007/s00253-002-1032-6.[50] J. H. Yu, N. Keller, Regulation of Secondary Metabolism in Filamentous Fungi, Annu Rev Phytopathol, Vol. 43, 2005, pp. 437-458, https://doi.org/10.1146/annurev.phyto.43.040204.140214.[51] J. F. Sanchez, A. D. Somoza, N. P. Keller, C. C. Wang, Advances in Aspergillus Secondary Metabolite Research in The Post-Genomic Era, Nat Prod Rep, Vol. 29, No. 3, 2012, pp. 351-371, https://doi.org/10.1039/c2np00084a.[52] J. W. Bennett, M. Klich, Mycotoxins, Clin Microbiol Rev, Vol. 16, 2003, pp. 497-516, https://doi.org/10.1128/cmr.16.3.497-516.2003.[53] Q. Zhou, J. K. Liao, Statins and cardiovascular Diseases: from Cholesterol Lowering to Pleiotropy, Curr Pharm Des, Vol. 15, No. 5, 2009, pp. 467-478, https://doi.org/10.2174/138161209787315684.[54] A. W. Alberts, Discovery, Biochemistry and Biology of Lovastatin, Am J Cardiol, Vol. 62, No. 15, 1988, pp. 10J-15J, https://doi.org/10.1016/0002-9149(88)90002-1.[55] H. Tomoda, Y. K. Kim, H. Nishida, R. Masuma, S. Omura, Pyripyropenes, Novel Inhibitors of Acyl-Coa: Cholesterol Acyltransferase Produced by Aspergillus Fumigatu- Production, Isolation, and Biological Properties, J Antibiot (Tokyo), Vol. 47, No. 2, 1994, pp. 148-153, https://doi.org/10.7164/antibiotics.47.148.[56] F. Pelaez, Biological Activities of Fungal Metabolites, Marcel Dekker, United Stated of America, 2004.[57] E. L. Dulaney, Penicillin Production by The Aspergillus Nidulans Group, Mycologia, Vol. 39, No. 5, 2018, pp. 582-586, https://doi.org/10.1080/00275514.1947.12017637.[58] T. T. Bladt, J. C. Frisvad, P. B. Knudsen, T. O. Larsen, Anticancer and Antifungal Compounds from Aspergillus, Penicillium and Other Filamentous Fungi, Molecules, Vol. 18, No. 9, 2013, pp. 11338-11376, https://doi.org/10.3390/molecules180911338.[59] Y. Wu, Y. Chen, X. Huang, Y. Pan, Z. Liu, T. Yan, W. Cao, Z. She, alpha-Glucosidase Inhibitors: Diphenyl Ethers and Phenolic Bisabolane Sesquiterpenoids from The Mangrove Endophytic Fungus Aspergillus Flavus QQSG-3, Mar Drugs, Vol. 16, No. 9, 2018, pp. 307-316, https://doi.org/10.3390/md16090307.

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