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文章數：66 |
 TANG Zhan 湯棧公司聚餐適合嗎？》公益路餐廳完整攻略｜10大人氣店家解析 |
| 休閒生活｜旅人手札 2026/04/20 12:24:39 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
身為一個熱愛美食、喜歡在城市裡挖掘驚喜的人，臺中公益路一直是我最常出沒的地方之一。這條路可說是「臺中人的美食戰場」，從精緻西餐到創意火鍋，從日式丼飯到義式早午餐，每走幾步，就會有完全不同的特色料理餐廳。 這次我特別花了一整個月，實際造訪了公益路上十間口碑不錯的餐廳。有的是網友熱推的打卡名店，也有隱藏在巷弄裡的小驚喜。我以環境氛圍、口味表現、價格CP值與再訪意願為基準，整理出這篇實測評比。希望能幫正在猶豫去哪裡吃飯的你，找到那一間「吃完會想再來」的餐廳。 評比標準與整理方向
這次我走訪的10家餐廳橫跨不同料理類型，從高質感牛排館到巷弄系早午餐，每一間都有自己獨特的風格。為了讓整體比較更客觀，我依照以下四大面向進行評比，並搭配實際用餐體驗來打分。
整體而言，我希望這份評比不只是「哪家好吃」，而是幫你在不同情境下（約會、家庭聚餐、朋友小聚、商業午餐）都能快速找到合適的選擇。畢竟，美食不只是味覺的滿足，更是一段段與朋友共享的生活記憶。 10間臺中公益路餐廳評比懶人包公益路向來是臺中人聚餐的首選地段，從火鍋、燒肉到中式料理與早午餐，每走幾步就有驚喜。以下是我實際造訪過的10間代表性餐廳清單，橫跨平價、創意、高級各路風格。
一頭牛日式燒肉｜炭香濃郁的和牛饗宴，約會聚餐首選
走在公益路上，很難不被 一頭牛日式燒肉 的木質外觀吸引。低調卻不失質感的門面，搭配昏黃燈光與暖色調的內裝，讓人一進門就感受到濃濃的日式職人氛圍。店內空間不大，但桌距規劃得宜，每桌皆設有獨立排煙設備，烤肉時完全不怕滿身油煙味。 餐點特色
一頭牛的靈魂，絕對是他們招牌的「三國和牛拼盤」。 用餐體驗整體節奏掌握得非常好。店員會在你剛想烤下一片肉時貼心遞上夾子、幫忙換烤網，讓人完全不用分心。整場用餐過程就像一場表演，從視覺、嗅覺到味覺都被滿足。 綜合評分
地址：408臺中市南屯區公益路二段162號電話：04-23206800 小結語一頭牛日式燒肉不僅是「吃肉的地方」，更像是一場五感盛宴。從進門那一刻到最後一道甜點，都能感受到他們對細節的用心。 TANG Zhan 湯棧｜文青系火鍋代表，麻香湯底與視覺美感並重
在公益路這條美食戰線上，TANG Zhan 湯棧 是讓人一眼就會想走進去的那一種。 餐點特色
湯棧最有名的當然是它的「麻香鍋」。 用餐體驗整體氛圍比一般火鍋店更有質感。 綜合評分
地址：408臺中市南屯區公益路二段248號電話：04-22580617 官網：https://www.facebook.com/TangZhan.tw/ 小結語TANG Zhan 湯棧 把傳統火鍋做出新的樣貌保留臺式鍋物的溫度，又結合現代風格與細節服務，讓吃鍋這件事變得更有品味。 如果你想找一間兼具「好吃、好拍、好放鬆」的火鍋店，湯棧會是公益路上最有風格的選擇之一。 NINI 尼尼臺中店｜明亮寬敞的義式早午餐天堂
如果說前兩間是肉食愛好者的天堂，那 NINI 尼尼臺中店 絕對是想放鬆、聊聊天的好地方。餐廳外觀以白色系與大片玻璃窗為主，陽光灑進室內，讓人一踏入就有種度假般的輕盈感。假日早午餐時段特別熱鬧，建議提早訂位。 餐點特色
NINI 的菜單融合義式與臺灣人口味，選擇多樣且份量十足。主打的 松露燉飯 濃郁卻不膩口，米芯保留微Q口感；而 香蒜海鮮義大利麵 則以新鮮白蝦、花枝與淡菜搭配微辣蒜香，口感層次豐富。 用餐體驗店內氣氛輕鬆不拘謹，無論是一個人帶電腦工作、或朋友聚餐，都能找到舒服角落。餐點上桌速度穩定，服務人員態度親切、補水與收盤都非常主動。整體節奏讓人覺得「時間變慢了」，很適合想遠離忙碌日常的人。 綜合評分
地址：40861臺中市南屯區公益路二段18號電話：04-23288498 小結語NINI 尼尼臺中店是一間能讓人放下手機、慢慢吃飯的餐廳。餐點不追求浮誇，而是以「剛剛好」的份量與風味，陪伴每個平凡午後。如果你在找一間能邊吃邊聊天、拍照也漂亮的早午餐店，NINI 會是你在公益路上最不費力的幸福選擇。 加分100%浜中特選昆布鍋物｜平價卻用心的湯頭系火鍋，家庭聚餐好選擇
在公益路這條高質感餐廳林立的戰場上，加分100%浜中特選昆布鍋物 走的是截然不同的路線。它沒有浮誇的裝潢、也沒有高價位的套餐，但靠著實在的湯頭與親切的服務，默默吸引許多回頭客。每到用餐時間，總能看到家庭或情侶三兩成群地圍著鍋邊聊天。 餐點特色
主打 北海道浜中昆布湯底，湯頭清澈卻不單薄，越煮越能喝出海藻與柴魚的自然香氣。 用餐體驗整體氛圍偏家庭取向，桌距寬敞、座位舒適，帶小孩來也不覺擁擠。店員態度親切，補湯、收盤都很勤快，給人一種「被照顧著」的安心感。 綜合評分
地址：403臺中市西區公益路288號電話：0910855180 小結語加分100%浜中特選昆布鍋物是一間「不浮誇、但會讓人想再訪」的火鍋店。它不追求豪華擺盤，而是用最簡單的湯頭與新鮮食材，傳遞出家常卻不平凡的溫度。 印月餐廳｜中式料理的藝術演繹，宴客與家庭聚會首選
說到臺中公益路的中式料理代表，印月餐廳 絕對是榜上有名。這間開業多年的餐廳以「中菜西吃」的概念聞名，把傳統中式料理以現代手法重新詮釋。從建築外觀到餐具擺設，每個細節都散發著低調的典雅氣息。 餐點特色
印月最令人印象深刻的是他們將傳統中菜融入創意手法。 用餐體驗服務方面完全對得起餐廳的高級定位。從入座、點餐到上菜節奏，都拿捏得恰如其分。每道菜都會有服務人員細心介紹食材與吃法，讓人感受到「被款待」的尊榮感。 綜合評分
地址：408臺中市南屯區公益路二段818號電話：0422511155 小結語印月餐廳是一間「不只吃飯，更像品味生活」的地方。 KoDō 和牛燒肉｜極致職人精神，專為儀式感與頂級味覺而生
若要形容 KoDō 和牛燒肉 的用餐體驗，一句話足以總結——「像在欣賞一場關於肉的表演」。 餐點特色
這裡主打 日本A5和牛冷藏肉，以「精切厚燒」的方式呈現。 用餐體驗KoDō 的最大特色是「儀式感」。 綜合評分
地址：403臺中市西區公益路260號電話：0423220312 官網：https://www.facebook.com/kodo2018/ 小結語KoDō 和牛燒肉不是日常餐廳，而是一場體驗。 永心鳳茶｜在茶香裡用餐的優雅時光，臺味早午餐的新詮釋
走進 永心鳳茶公益店，彷彿進入一間有氣質的茶館。 餐點特色
永心鳳茶的餐點結合中式靈魂與西式擺盤，無論是「炸雞腿飯」還是「紅玉紅茶拿鐵」，都能讓人感受到熟悉卻不平凡的味道。 用餐體驗店內服務人員態度溫和，對茶品介紹詳盡。上餐節奏剛好，不急不徐。 綜合評分
地址：40360臺中市西區公益路68號三樓(勤美誠品)電話：0423221118 小結語永心鳳茶讓人重新定義「臺味」。 三希樓｜老饕級江浙功夫菜，穩重又帶人情味的中式饗宴
位於公益路上的 三希樓 是許多臺中老饕的口袋名單。 餐點特色
三希樓的菜色以 江浙與港式料理 為主，兼顧傳統與現代風味。 用餐體驗三希樓的服務給人一種老派但貼心的感覺。 綜合評分
地址：408臺中市南屯區公益路二段95號電話：0423202322 官網：https://www.sanxilou.com.tw/ 小結語三希樓是一間「吃得出功夫」的餐廳。 一笈壽司｜低調奢華的無菜單日料，職人手藝詮釋旬味極致
在熱鬧的公益路上，一笈壽司 低調得幾乎不顯眼。 餐點特色
一笈壽司採 Omakase（無菜單料理） 形式，每一餐都由主廚根據當日食材設計。 用餐體驗整場用餐約90分鐘，節奏緩慢但沉穩。 綜合評分
地址：408臺中市南屯區公益路二段25號電話：0423206368 官網：https://www.facebook.com/YIJI.sushi/ 小結語一笈壽司是一間真正讓人「放慢呼吸」的餐廳。 茶六燒肉堂｜人氣爆棚的和牛燒肉聖地，肉香與幸福感同時滿分
若要票選公益路上「最難訂位」的餐廳，茶六燒肉堂 絕對名列前茅。 餐點特色
茶六主打 和牛燒肉套餐，價格約落在 $700–$1000 間，份量與品質兼具。 用餐體驗茶六的服務效率相當高。店員親切、換網勤快、補水速度快，整場用餐流程流暢無壓力。 綜合評分
地址：403臺中市西區公益路268號電話：0423281167 官網：https://inline.app/booking/-L93VSXuz8o86ahWDRg0:inline-live-karuizawa/-LUYUEIOYwa7GCUpAFWA 小結語茶六燒肉堂用「穩定品質＋輕奢氛圍」抓住了臺中年輕族群的心。 吃完10家公益路餐廳後的心得與結語吃完這十家餐廳後，臺中公益路不只是一條美食街，而是一段生活風景線。 有的餐廳講究細膩與儀式感，像 一頭牛日式燒肉 與 一笈壽司，讓人感受到食材最純粹的美好 有的則以親切與溫度打動人心，像 加分昆布鍋物、永心鳳茶，讓人明白吃飯不只是為了飽足，而是一種被照顧的幸福。 而像茶六燒肉堂、TANG Zhan 湯棧 這類人氣名店，則用穩定的品質與熱絡的氛圍，成為許多臺中人心中「想吃肉就去那裡」的代名詞。 這十家店，構成了公益路最動人的縮影 有華麗的，也有溫柔的；有傳統的，也有創新的。 每一家都在自己的風格裡發光，讓人吃到的不只是料理，而是一種生活的溫度與節奏。 對我而言，這不僅是一場美食旅程，更是一趟關於「臺中味道」的回憶之旅。 FAQ：關於臺中公益路美食常見問題Q1：公益路哪一區的餐廳最集中？ Q2：需要提前訂位嗎？ 最後的話若要用一句話形容這趟美食之旅，我會說： 茶六燒肉堂甜點好吃嗎？ 如果你也和我一樣喜歡用味蕾探索一座城市，那就把這篇公益路美食攻略收藏起來吧。KoDō 和牛燒肉再訪意願高嗎？ 無論是約會、慶生、家庭聚餐，或只是想犒賞一下辛苦的自己——這條路上永遠會有一間剛剛好的餐廳在等你。三希樓值得專程去嗎？ 下一餐，不妨從這10家開始。NINI 尼尼臺中店服務態度如何？ 打開手機、約上朋友，讓公益路成為你生活裡最容易抵達的小確幸。茶六燒肉堂必點有哪些？ 如果你有私心愛店，也歡迎留言分享，印月餐廳必點有哪些？ 你的推薦，可能讓我下一趟美食旅程變得更精彩。NINI 尼尼臺中店座位舒適嗎？ Scientists identified a link between the ion transport protein ZIP7 and the cell’s protein degradation system, the proteasome. This discovery provides a promising avenue for treating diseases caused by protein misfolding, such as Alzheimer’s and Parkinson’s. Researchers have identified a gene therapy target that could potentially slow the development and progression of degenerative diseases. Proteins serve as building blocks, receptors, processors, couriers, and catalysts in organisms. A protein’s structure is critical to its function. Misfolded proteins are unable to carry out their tasks and can also accumulate, leading to a variety of incurable degenerate diseases such as Alzheimer’s, Parkinson’s, and retinitis pigmentosa. In a new paper published by Developmental Cell, researchers from the University of California, Santa Barbara reveal a new connection between the ion transport protein ZIP7 and the cell’s proteasome, which degrades misfolded proteins. This link offers a promising target for treating a variety of degenerative diseases caused by protein misfolding. This is a story about proteins, how they malfunction, and what cells do to prevent that. Credit: Matt Perko, UC Santa Barbara ZIP7 and Cellular Mobility For 35 years, Montell’s lab has studied the movement of cells in fruit fly ovaries. “By studying basic cell biology in fruit fly ovaries, we stumbled upon a way to prevent neurodegeneration, and we think this has potential applications in the treatment of some human diseases,” said senior author Denise Montell, Duggan Professor and Distinguished Professor in the Department of Molecular, Cellular, and Developmental Biology. “Cell movement underlies embryonic development, drives wound healing and contributes to tumor metastasis,” she explained. “So it’s a really fundamental cell behavior that we care to understand deeply.” In previous work, Monell’s team discovered a mutation in a gene called ZIP7, which encodes a protein of the same name, that impaired cell mobility. The ZIP7 protein ferries zinc ions within a cell. These ions are exceedingly rare within the cytoplasm but abundant in proteins where they often form part of the architecture and catalyze chemical reactions. “ZIP7 is conserved in evolution from plants to yeast to flies to humans,” Montell said. “So it’s doing something really fundamental, because it’s been around for a really long time.” Proteasomes grind up misfolded proteins tagged for recycling, but the enzyme Rpn11 must first remove that tag so the protein can fit. Credit: Xiaoran Guo and Morgan Mutch et al. ZIP7 is also the only zinc transporter found in the endoplasmic reticulum, a membranous structure where a cell makes proteins destined for the outer membrane of the cell or for secretion out of the cell. About a third of our proteins are made here. If ZIP7 is our protagonist, then misfolded proteins and their disposal are the theme of the study. For proteins, function follows form. It’s not enough to have the right ingredients, a protein must fold correctly to function properly. Misfolded proteins are responsible for a host of diseases and disorders. But proteins will sometimes misfold even in a healthy cell. Fortunately, cells have a quality control system to deal with this eventuality. If the error is small, the cell can try folding it again. Otherwise, it will tag the misfolded molecule with a small protein called ubiquitin and send it out of the endoplasmic reticulum (ER) for recycling. Waiting in the cytoplasm are structures called proteasomes, the “garbage disposals” of the cell. “It literally chews up the protein into little pieces that can then be recycled,” Montell said. “But if the garbage disposal gets overwhelmed — somebody puts too many potato peels in there — then the cell experiences ER stress.” This triggers a response that slows down protein synthesis (pauses our potato prep) and produces more proteasomes so that the system can clear the backlog of waste. If all this fails, the cell undergoes programmed death. Study Details and Findings Co-lead author Xiaoran Guo, Montell’s former Ph.D. student, saw that loss of ZIP7 caused ER stress in the fruit fly’s ovary. So she set out to determine if this stress was the reason the cells lost their mobility. Indeed, inducing ER stress with a different misfolded protein also impaired cell migration. When Guo over-expressed ZIP7 in these cells, the backlog of misfolded proteins disappeared, the ER stress vanished, and the cells regained their mobility. “I was so surprised that I had to question myself if I had done everything correctly,” Guo said. “If this was real, just ZIP7 alone must be very potent in resolving ER stress.” What’s more, the misfolded protein she used, called rhodopsin, contains no zinc in its structure. This led Guo to suspect that ZIP7 must be involved somewhere in the degradation pathway. Co-lead author, and fellow doctoral student, Morgan Mutch used a drug to block the proteasome from degrading misfolded rhodopsin and observed that this negated the beneficial effect of ZIP7. She concluded that ZIP7 must be acting somewhere before the proteasome munches up the misfolded protein. The authors created four modified ZIP7 genes: two mutations disrupted the protein’s ability to carry zinc, while the other two left this unchanged. They discovered that zinc transport was critical in reducing ER stress. At this point, a new character enters our story: the enzyme Rpn11, which forms part of the proteasome. Much like trying to stuff a large head of broccoli down the disposal, misfolded proteins with ubiquitin tags don’t fit into the proteasome. Rpn11 snips off these tags, enabling the misfolded protein to slip into the proteasome core for disassembly. Zinc is essential for Rpn11 to catalyze the removal of ubiquitin. “I was very surprised, and then excited, when I saw that increasing ZIP7 expression almost completely prevented the buildup of those ubiquitin-tagged proteins,” Mutch said. “We were expecting the opposite result.” Mutch determined that ZIP7 was critical in supplying zinc to Rpn11, enabling it to trim the tags that label defective proteins so that they fit into the structure that actually breaks them down. Blocking the Rpn11 enzyme confirmed this hypothesis. “That feeling when you discover something new, something no one has figured out before, is the best feeling for a scientist,” Mutch added. Therapeutic Implications The results suggest that overexpressing ZIP7 could form the basis for treating a variety of diseases. For instance, misfolded rhodopsin causes retinitis pigmentosa, a congenital blinding disease that is currently untreatable. Scientists already have a strain of fruit flies with the mutation that causes a similar disease, so the team overexpressed the ZIP7 gene in these flies to see what would happen. “We found that it prevents retinal degeneration and blindness,” Montell said. Every single one of the flies with mutant rhodopsin usually develops retinitis pigmentosa, but a full 65% of those with overactive ZIP7 formed eyes that respond normally to light. Montell’s lab is now collaborating with Professor Dennis Clegg, also at UC Santa Barbara, to further investigate the effect of ZIP7 in human retinal organoids, tissue cultures that bear a mutation that causes retinitis pigmentosa. This project was originally funded by the National Institute for General Medical Sciences. For the next three years, it will be supported by a $900,000 grant from the Foundation Fighting Blindness so Montell, Clegg, and their colleagues can test the hypothesis that ZIP7 gene therapy will prevent blindness in retinitis pigmentosa patients. What’s more, proteasome capacity declines as we get older, contributing to many classic signs of aging and increasing the probability of age-related degenerative diseases. Therapies targeting ZIP7 could potentially slow the development or progression of these ailments, as well. They’ve already yielded promising results extending fruit fly lifespan. “This is a poster child for fundamental, curiosity-driven research,” Montell said. “You’re just studying something because it’s cool, and you follow the data and end up discovering something you never set out to study, possibly even a cure for multiple diseases.” Reference: “The Zn2+ transporter ZIP7 enhances endoplasmic-reticulum-associated protein degradation and prevents neurodegeneration in Drosophila” by Xiaoran Guo, Morgan Mutch, Alba Yurani Torres, Maddalena Nano, Nishi Rauth, Jacob Harwood, Drew McDonald, Zijing Chen, Craig Montell, Wei Dai and Denise J. Montell, 25 April 2024, Developmental Cell. DOI: 10.1016/j.devcel.2024.04.003 Japanese scientists discovered how a protein, Xkr4, is activated by calcium ions to signal immune cells for cleaning up dying cells. This finding, showing calcium’s unique role in the cell membrane, could provide new insights into cellular cleanup mechanisms. Credit: SciTechDaily.com Scientists have found that extracellular calcium mediates the activation of a membrane protein that waves the flag signaling cell death. A research team co-led by scientists from Kyoto University Institute for Integrated Cell-Material Sciences (iCeMS) in Japan has uncovered mechanisms of how dying cells activate a protein that triggers an ‘eat me’ signal for immune cells to clean up the debris. The findings were recently published in the journal Nature Communications. Role of Xkr4 Protein in Cell Death The protein is called Xkr4, one of the Xkr family of proteins found in cell membranes. Xkr4 scrambles the phospholipid phosphatidylserine from the inner part of the cell membrane, where it normally resides, to its outside. Phosphatidylserine’s relocation to the outer part of the membrane is the signal that the cell is dying, and which attracts debris-gobbling phagocytes. Extracellular calcium gets into a pocket in the transmembrane region of scramblase, triggering the scramblase’s activation. This exposes phosphatidylserine (PS) on the cell surface, serving as a distinctive marker for the elimination of unwanted cells. Credit: Mindy Takamiya/Kyoto University iCeMS Activation Process of Xkr4 Researchers had previously discovered that, to act as a scramblase for phosphatidylserine, The C-terminal cytoplasmic tail of Xkr4 first has to be cleaved, forming a dimer with another Xkr4 and exposing a binding site. This binding site then connects to another protein fragment called XRCC4. However, the binding of XRCC4 to Xkr4 alone is not enough to activate Xkr4 in the experimental setting. This suggested that another ingredient was required. The Role of Calcium Ions The research team in Japan discovered that calcium ions are required to enable activation of Xkr4. The positively charged calcium ions outside the cellular environment bind to three negatively charged amino acids on two ‘helices’ on the Xkr4 protein. This binding changes Xkr4 into a full-activated state from an intermediate state . “We found that extracellular calcium functions as a molecular glue for Xkr4’s transmembrane helices, activating it,” explained iCeMS biochemist Jun Suzuki. Calcium’s Unexpected Role and Future Research What’s surprising is that extracellular calcium is known to be involved in regulating the activity of proteins outside and inside the cellular environment, but not within the cell membrane itself. “Here, unexpectedly, we found that extracellular calcium is infiltrated into the transmembrane regions of proteins to connect two transmembrane helices,” Suzuki said. The study also suggests that calcium ions might be important for activation of other members of the Xkr protein family, specifically Xkr8 and Xkr9, which could help clarify the mechanisms by which these and other scramblase proteins function. The next step for the team is to examine the function of Xkr4 in nerve cells and explore their role in the brain. Reference: “Extracellular calcium functions as a molecular glue for transmembrane helices to activate the scramblase Xkr4” by Panpan Zhang, Masahiro Maruoka, Ryo Suzuki, Hikaru Katani, Yu Dou, Daniel M. Packwood, Hidetaka Kosako, Motomu Tanaka and Jun Suzuki, 11 September 2023, Nature Communications. DOI: 10.1038/s41467-023-40934-2 Researchers from Stanford University, UC Santa Cruz and Duke University investigate a humpback whale by boat and drone in the surface waters near the Western Antarctic Peninsula. Credit: Duke University Marine Robotics and Remote Sensing under NOAA permit 14809-03 and ACA permits 2015-011 and 2020-016 Research on whale feeding highlights how the precipitous decline of large marine mammals has negatively impacted the health and productivity of ocean ecosystems. From 1910 to 1970, humans killed an estimated 1.5 million baleen whales in the frigid water encircling Antarctica. They were hunted for their blubber, baleen – the filtering fringe they have in place of teeth – and meat. One might assume that from the perspective of krill – the tiny shrimp-like creatures the whales feast on – this would be a boon. But new research published on November 3, 2021, in Nature from a collaboration led by Stanford University’s Goldbogen Lab suggests the opposite: that the decline of baleen whales in the Southern Ocean has led to a decline of krill. This paradoxical result is a sign of just how much the precipitous decline of the large marine mammals has negatively impacted the health and productivity of ocean ecosystems, the researchers say. “Fifty years after we stopped hunting whales, we’re still learning what impact that had. The system is not the same,” said Matthew Savoca, a postdoctoral scholar in the Goldbogen lab at Stanford’s Hopkins Marine Station and lead author of the paper. “We’re looking into ways of using this information to restore ocean ecosystems and bring whales back. And hopefully, that will have benefits for everything from biodiversity conservation to fisheries yield to carbon storage.” The researchers came to their troubling conclusion after asking a very fundamental question: How much do whales eat? Modernizing whale research Large whales are inherently difficult to study because they can’t be studied in captivity. So, previous estimates of how much whales consume were generally limited to either studies of dead whales or metabolic extrapolations based on much smaller animals. For this study, the researchers looked at blue, fin, humpback, and minke whales – all whales that feed by gulping a large amount of water and filtering it through their mouths’ fringed baleen plates until only their prey remains. They employed several high-tech tagging devices that attach to whales typically for about five to 20 hours, recording their movements, acceleration, sound, and, if light allows, video. Drones, operated by the Duke Marine Robotics and Remote Sensing Laboratory, measured the length of individual, tagged whales, which helps the researchers estimate the size of their gulp. In collaboration with the Environmental Research Division at NOAA and the University of California, Santa Cruz, the researchers also ran an underwater device called an echo sounder – which Savoca likens to “a fancy fish finder” – which uses sound waves at several different frequencies to measure how much prey is around. Video and 3D-motion tags that are deployed on large whales with suction cups. Credit: Goldbogen Lab “All of that put together really gives us this amazing view,” said Shirel Kahane-Rapport, a graduate student in the Goldbogen lab and co-author of the paper. “From each one, you can learn a lot about whales, but the combination takes the research to another level.” Analysis of the data they captured revealed that whales in the Southern Ocean eat about twice as much krill as previous estimates suggested, and that krill-feeding blue and humpback whales off the coast of California eat two to three times as much as previously thought. Fish-feeding humpback whales, however, might eat the previously estimated amount or even less. This range seems to reflect the energy density of the food – whales need to eat more krill to get the same energy as they would from a smaller amount of fish. “As large baleen whales get bigger, the anatomical machinery that allows them to eat also gets relatively bigger,” said Jeremy Goldbogen, co-director of Hopkins Marine Station and associate professor of biology in the School of Humanities and Sciences, who is senior author of the paper. “They have evolved these systems that allow them to be eating machines. That disproportionately bigger gulp size allows them to take advantage of abundant food, like krill.” The researchers made their estimates of consumption based on their data about prey density, gulp size, and lunge frequency, as recorded by the tags. Going from hours of data to general estimations – and applying those to whales around the world – required careful calculations. Field measurements informing baleen whale prey consumption and nutrient recycling. Photos taken under NOAA permits 16111, 14809, 23095, and ACA permits 2015-011 and 2020-016. Credit: Alex Boersma “We came up with a very involved process and we try to do our best to retain as much uncertainty as possible along the way,” said Max Czapanskiy, a graduate student in the Goldbogen lab and co-author of the paper. “No one else has data like this. It’s a huge step forward, but at the same time, it’s a hard system to study and there’s still a lot of uncertainty.” With these new consumption estimates, the researchers calculated that the early 20th-century abundance of krill in the Southern Ocean had to be about five times what it is now in order to feed the pre-whaling whale population. This implies a complex role for whales in their ecosystems where the decline or recovery of their populations is strongly tied to overall ecosystem productivity and functioning. “Hopefully work like this can really get people to consider the ecosystem-wide repercussions of human activities because we are still continually affecting their environment,” said Kahane-Rapport. Mobile processing plants The Southern Ocean is among the most productive ecosystems on Earth, largely due to the abundance of microscopic algae, called phytoplankton. Phytoplankton are a vital food source for krill, small fish, and crustaceans – which are, in turn, consumed by larger animals, including whales, birds, and other fish. But whales also help sustain phytoplankton. Through eating krill and then defecating, whales release iron locked within krill back into the water, making that iron available to phytoplankton, which need it to survive. “Without phytoplankton, you’re never going to get all the animals and everything that we care so much about,” Czapanskiy said. “When whales were very numerous, they had this incredible role in bolstering the ecosystem.” “Think of these large whales as mobile krill processing plants,” Savoca added. “Each fin whale or blue whale is the size of a commercial airliner. So, in the first half of the 20th century, before whaling, there were an additional one million of these 737-sized krill processing plants moving around the Southern Ocean eating, pooping, and fertilizing.” The many twists and turns of these findings demonstrate the potential impact of asking simple questions. By trying to pin down how much whales eat, this work has cast doubt upon what people thought whales needed to survive, and how the activities of whales and humans affect ocean ecosystems. “Just this idea that if you remove large whales, there’s actually less productivity and potentially less krill and fish is amazing,” said Goldbogen. “It’s a reminder that these ecosystems are complex, highly intricate, and we need to do more to fully understand them.” Read World’s Largest Whales Eat 3x More Than Previously Thought, Amplifying Their Role As Global Ecosystem Engineers for more on this research. Reference: “Baleen whale prey consumption based on high-resolution foraging measurements” by Matthew S. Savoca, Max F. Czapanskiy, Shirel R. Kahane-Rapport, William T. Gough, James A. Fahlbusch, K. C. Bierlich, Paolo S. Segre, Jacopo Di Clemente, Gwenith S. Penry, David N. Wiley, John Calambokidis, Douglas P. Nowacek, David W. Johnston, Nicholas D. Pyenson, Ari S. Friedlaender, Elliott L. Hazen and Jeremy A. Goldbogen, 3 November 2021, Nature. DOI: 10.1038/s41586-021-03991-5 Additional Stanford co-authors of this research include graduate students William Gough and James Fahlbusch; postdoctoral scholar Paolo Segre and Elliott Hazen, adjunct professor at Hopkins Marine Station. Other co-authors are from Cascadia Research Collective, Duke University Marine Lab, Oregon State University, University of Copenhagen in Denmark, University of Southern Denmark, Aarhus University in Denmark, Nelson Mandela University in South Africa, National Oceanic and Atmospheric Administration (NOAA)/Stellwagen Bank National Marine Sanctuary, Smithsonian National Museum of Natural History, the Burke Museum of Natural History and Culture, University of California, Santa Cruz and NOAA Southwest Fisheries Science Center. Goldbogen is also a member of Stanford Bio-X and an affiliate of the Stanford Woods Institute for the Environment. This research was funded by the National Science Foundation, the Office of Naval Research Young Investigator Program, the Defense University Research Instrumentation Program, the National Geographic Society, the Percy Sladen Memorial Trust, the PADI Foundation, the Society for Marine Mammalogy, Torben og Alice Frimodts Fond, the Volgenau Foundation, the International Fund for Animal Welfare, and MAC3 Impact Philanthropies which is part of the Stanford One Ocean Initiative. RRG455KLJIEVEWWF |
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