Activity and stability ofPenicillium cyclopium lipase in surfactant and detergent solutions

Activity and stability of an alkaline lipase fromPenicillium cyclopium var.album (PG 37) were studied in surfactant and detergent solutions. Three anionic surfactants [Na salts of C₁₂SO₄ ^? (sodium dodecyl sulfate), C₁₂ØSO₃/^? (linear alkyl benzene sulfonate), and C₁₁COO^? (laurate)] and four homologous series of nonionic surfactants of C_12–15 polyoxethylenated fatty alcohols (AEO₃, AEO₅, AEO₇, and AEO₉) were evaluated. At a concentration range of 3.2–40 μM, sodium dodecyl sulfate and laurate stimulated the activity of PG 37 lipase. At concentrations greater than 5.6 μM, linear alkylbenzene sulfonate inhibited PG 37 lipase activity. Nonionic surfactants, AEO₅ and AEO₇, in the concentration range of 0.25–20 mM, enhanced and stabilized the activity of PG 37 lipase. The presence of PG 37 lipase in detergent formulaton improved detergency ～20%. The mechanism of inhibition of the lipolytic activity of PG 37 lipase is proposed to be partly due to the formation of inactive (BR)_n-E complex between the hydrophobic moiety of the surfactants and the surface of the lipase. Conversely, formation of a soluble (RB)_n-E complex between the hydrophilic group of the surfactant and lipase may account for the increased lipolytic activity of PG 37 lipase.     

脂肪酶水解L-亮氨酸异丁酯的工艺

以脂肪酶A为催化剂,水解L-亮氨酸异丁酯制备L-亮氨酸。研究了不同酶、缓冲液体系、物料比、反应温度、反应时间对L-亮氨酸收率的影响,通过正交试验确定了L-亮氨酸异丁酯最佳水解条件。以L-亮氨酸异丁酯为原料,在提取脂肪酶液为Gly-NaOH缓冲液体系、反应前添加L-亮氨酸达到L-亮氨酸溶解度的质量、物料比为1∶13、50℃、摇床转速为170r/min的条件下反应13h,L-亮氨酸的收率为95.23%。     

酶催化合成高纯度甘油中碳酸单酯

研究了无溶剂体系中脂肪酶LRI催化合成甘油中碳酸单酯(MG)。得到适宜的反应条件为:反应温度57℃,n(酸)∶n(甘油)=1∶1 1,加酶量100U/g(酸),甘油初始含水量w(H2O)=12%,封闭物系反应4h转敞开物系反应6h。产物中甘油中碳酸单酯质量分数w(MG)=42 20%。将n(酸)∶n(甘油)降低至1∶9,反应时间缩短至4h,粗产物经脱甘油和脱酸处理,可获得高纯度甘油中碳酸单酯。纯化后产品中基本不含游离酸及甘油,其中甘油中碳酸单酯质量分数w(MG)=73 65%。过量加入的甘油全部可以回收利用,其平衡转化率降低不超过2%。     

碱性脂肪酶生产菌假单孢菌4631菌株的筛选

从３２个土样中分离获得碱性脂肪酶产生菌１６６株，其中４６３１号菌株产酶能力最高，达到９．１ＩＵ／ｍｌ。初步鉴定为假单孢菌属。对研究结果统计分析表明，Ｄ／ｄ值与ＬＡ呈线性相关关系。     

Lipase catalyzed synthesis of polycaprolactone and clay-based nanohybrids

This study presents the use of original systems based on Candida antarctica lipase B (CALB) immobilized on montmorillonite and sepiolite nanoclays as efficient catalysts for the enzymatic polymerization of ε-caprolactone (ε-CL) and the in situ elaboration of nanohybrids.     

Effect of dry‐heat treatments on the nutritional value of maize germ

Maize germ is a by‐product of the maize milling process that is characterised by a high nutritional value. Currently, heat treatments are employed to prevent full‐fat maize germ from spoilage. The aim of this research was to study the effect of five dry‐heat treatments on the nutritional value of full‐fat maize germ. The results confirmed that after each dry‐heat treatment, the lipase activity decreases but the use of high temperatures could be detrimental for phytosterol and thiamine concentrations. The main negative effects have been observed after treatments at 140 °C for 30 min and 160 °C for 10 min. No significant difference has been observed for protein, ash or fatty acid contents. The treatment at 140 °C for 20 min resulted an optimal combination between temperature and heating time to inactivate lipase without altering deeply the nutritional value and the colour of maize germ.     

Polyphenols Extracted from Black Tea (Camellia sinensis) Residue by Hot‐Compressed Water and Their Inhibitory Effect on Pancreatic Lipase in vitro

Abstract: Polyphenols, retained in black tea wastes following the commercial production of tea beverages, represent an underutilized resource. The purpose of this study was to investigate the potential use of hot‐compressed water (HCW) for the extraction of pancreatic lipase‐inhibiting polyphenols from black tea residues. Black tea residues were treated with HCW at 10 °C intervals, from 100 to 200 °C. The resulting extracts were analyzed using high‐performance liquid chromatography‐mass spectrometry and assayed to determine their inhibitory effect on pancreatic lipase activity in vitro. Four theaflavins (TF), 5 catechins, 2 quercetin glycosides, quinic acid, gallic acid, and caffeine were identified. The total polyphenol content of extracts increased with increasing temperature but lipase inhibitors (TF, theaflavin 3‐O‐gallate, theaflavin 3′‐O‐gallate, theaflavin 3,3′‐O‐gallate, epigallocatechin gallate, and epicatechin gallate) decreased over 150 °C. All extracts inhibited pancreatic lipase but extracts obtained at 100 to 140 °C showed the greatest lipase inhibition (IC₅₀s of 0.9 to 1.3 μg/mL), consistent with the optimal extraction of TFs and catechins except catechin by HCW between 130 and 150 °C. HCW can be used to extract pancreatic lipase‐inhibiting polyphenols from black tea waste. These extracts have potential uses, as dietary supplements and medications, for the prevention and treatment of obesity. Practical Application: Active forms of lipase inhibitors can be recovered from black tea residues. They could be used as dietary supplements or medications.     

Hepatic patatin-like phospholipase domain-containing protein 3 sequence,single nucleotide polymorphism presence,protein confirmation,and responsiveness to energy balance in dairy cows

Patatin-like phospholipase domain-containing protein 3 (PNPLA3), commonly known as adiponutrin, is part of a novel subfamily of triglyceride lipase enzymes with potential effects on triglyceride metabolism in adipose and hepatic tissues. The predicted bovine PNPLA3 sequence has been identified, but expression of the gene had not been examined. The objectives of this study were to confirm the predicted bovine PNPLA3 gene sequence, determine expression of the bovine PNPLA3 gene in response to whole-animal energy balance, identify single nucleotide polymorphisms present in dairy cows, and verify the presence of the protein in the liver. Using liver biopsy samples collected from cows at +28 d relative to calving (DRTC), RNA was isolated and used to generate a cDNA template for amplification of the entire predicted coding sequence of PNPLA3 via PCR. To determine if energy balance alters the expression of PNPLA3, RNA was isolated and mRNA expression quantified in liver samples from mid-lactation cows after a 5-d ad libitum period (n = 5) and after a subsequent 5-d 50% feed restriction period (n = 5), and in samples collected from cows at −14, +1, +14, and +28 DRTC (n = 16). The presence of PNPLA3 protein was detected by Western blot in liver protein samples collected at +28 DRTC. Expression of hepatic PNPLA3 was decreased after a period of feed restriction (8.14 vs. 1.08 ± 2.17 arbitrary units, ad libitum vs. fasted). Expression of PNPLA3 mRNA was decreased at +1 and +14 DRTC compared with −14 DRTC (23.35, 7.28, 10.17, and 14.5 ± 4.9 arbitrary units, −14, +1, +14, and +28 DRTC, respectively). The presence of PNPLA3 protein was detected as a 55-kDa band in hepatic protein isolations from liver tissue collected at +28 DRTC. These data confirm the presence and sequence of the bovine hepatic PNPLA3 gene and single nucleotide polymorphisms. Furthermore, these data indicate responsiveness of bovine hepatic PNPLA3 to energy balance.     

High Yield of Wax Ester Synthesized from Cetyl Alcohol and Octanoic Acid by Lipozyme RMIM and Novozym 435

Wax esters are long-chain esters that have been widely applied in premium lubricants, parting agents, antifoaming agents and cosmetics. In this study, the biocatalytic preparation of a specific wax ester, cetyl octanoate, is performed in n-hexane using two commercial immobilized lipases, i.e., Lipozyme^® RMIM (Rhizomucor miehei) and Novozym^® 435 (Candida antarctica). Response surface methodology (RSM) and 5-level-4-factor central composite rotatable design (CCRD) are employed to evaluate the effects of reaction time (1–5 h), reaction temperature (45–65 °C), substrate molar ratio (1–3:1), and enzyme amount (10%–50%) on the yield of cetyl octanoate. Using RSM to optimize the reaction, the maximum yields reached 94% and 98% using Lipozyme^® RMIM and Novozym^® 435, respectively. The optimum conditions for synthesis of cetyl octanoate by both lipases are established and compared. Novozym^® 435 proves to be a more efficient biocatalyst than Lipozyme^® RMIM.